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Meat and glycation inhibitors


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#1 Skötkonung

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Posted 10 December 2009 - 07:22 PM


I thought that since meat is often touted to contain glycation inhibitors, I would look for any confirming this assertion. I have pulled studies referring to the presence of carnosine in beef or other meats, both used as a packaging element or as a inherent antioxidant.

Carnosine:

Study: Quantitation of Carnosine in Humans Plasma after Dietary Consumption of Beef
"Carnosine (β-alanyl-l-histidine) is a dipeptide found in the muscle foods that has been postulated to be a bioactive food component. The objective of this research was to determine the concentration of carnosine in human plasma after ingestion of beef. Nine males and nine females were recruited for the study. Food devoid of meat products was given to the subjects so that they did not consume carnosine for 48 h prior to the test. Subjects fasted for 12 h and then had blood withdrawn prior to a meal containing 200 g of ground beef. Additional blood samples were collected over the following 24 h and carnosine concentrations were determined by HPLC. The cooked ground beef used in the study contained 52% water, 24% protein, 22% fat, and 124 mg of carnosine/100 g of beef. No plasma carnosine was detected in subjects before the consumption of the beef. Carnosine was detected in plasma 15 min after beef consumption. Plasma carnosine concentrations continued to increase with a maximum (32.7 mg of carnosine/L of plasma) being recorded 2.5 h after consumption. Carnosine concentrations then decreased until no carnosine could be detected at 5.5 h postconsumption. These results indicate that dietary carnosine is absorbed into human plasma after the consumption of beef. Since carnosine has several potential health benefits, evidence of its bioavailability suggests that it could be a bioactive food component."

Study: The effects of ascorbic acid, taurine, carnosine and rosemary powder on colour and lipid stability of beef patties packaged in modified atmosphere
"This research was aimed at evaluating the inhibition of oxidative changes of beef patties packaged in modified atmosphere (70% O2+20% CO2+10% N2) by natural antioxidants: ascorbic acid (500 ppm), taurine (50 mM), carnosine (50 mM), rosemary powder (1000 ppm) and their combinations with the first. Beef patties stored at 2±1°C for 20 days were evaluated for colour (L*, a*, b*, C* and H*), TBARS, metmyoglobin formation (% of total myoglobin), psychrotrophic microbial counts and sensory odour and discolouration. Rosemary, either alone or with ascorbic acid, was highly effective in inhibiting both metmyoglobin formation and lipid oxidation; sensory analysis was in agreement with these results. Ascorbic acid, ascorbic acid+taurine and ascorbic acid+carnosine treatments showed a limited inhibitory effect of myoglobin oxidation, while carnosine and carnosine+ascorbic acid were effective in inhibiting lipid oxidation. Taurine alone failed to exert any antioxidant effect. Principal components analysis confirmed these results."

Study: Antioxidant effect of carnosine and carnitine in fresh beef steaks stored under modified atmosphere
"The exogenous aplication of carnosine (β-alanine-L-histidine) (50 mM), carnitine (50 mM) and L-ascorbic acid (500 ppm) solutions on the shelf life of fresh beef steaks packaged in modified atmosphere (70% O2+20% CO2+10% N2) was studied. Beef steaks were sprayed with natural antioxidant solutions at a ratio of 2 ml solution to 100 g meat. Lipid oxidation (TBARS formation), colour changes (CIE a* value and metmyoglobin formation), antimicrobial properties (psychrotrophic flora), and sensory (off odour and discolouration) changes were examined throughout 28 days of storage. Results showed that the combination of carnosine with ascorbic acid provided the best antioxidative protection with regard to meat deterioration. Surface aplication of carnosine or ascorbic acid alone resulted in an effective delay of oxidation of meat. However, carnitine was significantly (P<0.05) less effective than any other antioxidant in delaying meat oxidation, while the combination of carnitine and ascorbic acid exerted no antioxidant effect."

Study: Concentrations in beef and lamb of taurine, carnosine, coenzyme Q10, and creatine
"Levels of taurine, carnosine, coenzyme Q10, and creatine were measured in beef liver and several muscles of beef and lamb and in cooked and uncooked meat. The amino acid taurine has numerous biological functions, the dipeptide carnosine is a buffer as well as an antioxidant, coenzyme Q10 is also an antioxidant present within mitochondria, and creatine along with creatine phosphate is involved with energy metabolism in muscle. Large differences were shown for all compounds between beef cheek muscle (predominantly red fibres) and beef semitendinosus muscle (mainly white fibres), with cheek muscle containing 9.9 times as much taurine, and 3.2 times as much coenzyme Q10, but only 65% as much creatine and 9% as much carnosine. Levels in lamb relative to beef semitendinosus muscles were higher for taurine but slightly lower for carnosine, coenzyme Q10 and creatine. Values for all the compounds varied significantly between eight lamb muscles, possibly due in part to differences in the proportion of muscle fibre types. Slow cooking (90 min at 70 °C) of lamb longissimus and semimembranosus muscles led to significant reductions in the content of taurine, carnosine, and creatine (P<0.001), but a slight increase in coenzyme Q10. There was also a four-fold increase in creatinine, presumably due to its formation from creatine. It is concluded that biologically, and possibly nutritionally, significant levels of taurine, carnosine, coenzyme Q10, and creatine are present in beef and lamb, but that these levels vary between muscles, between animals, and with cooking."

Study: The effect of production system and age on levels of iron, taurine, carnosine, coenzyme Q10, and creatine in beef muscles and liver
"Samples of longissimus (LL) and triceps brachii (TB) muscles from Angus-cross heifers finished either on a high-concentrate ration in Washington, USA, (US cattle, n = 15) or on pasture in New Zealand (NZ cattle, n = 16) were assessed for composition characteristics. Half of the NZ cattle were of a similar age to the US cattle (NZAge) and half were of a similar weight (NZWt). Iron concentration was higher in TB (20.9 vs. 17.5 μg g−1; P < 0.001) and was higher for the NZWt group than the NZAge group or the US cattle. The proportion of iron as haem iron was highest for the NZWt group (87.3%; P < 0.01), but the proportion as soluble haem iron was highest for the US cattle. For a sub-group of 10 pasture-finished cattle, iron levels in cheek muscle were higher than for LL or TB, and liver levels were 66% higher than cheek muscle. The proportion of haem iron, however, was lowest in liver (55.3%) and was lower in cheek muscle (78.4%) than LL or TB. Relative to LL, TB had higher levels of taurine and coenzyme Q10, but lower levels of carnosine, creatine and creatinine, as expected for a muscle with a more aerobic metabolism. These differences were magnified for the even more aerobic cheek muscle. Differences between the two NZ groups were small, but muscles from the US cattle contained less taurine, carnosine, coenzyme Q10, and creatinine. Reasons for these differences in various meat components for similar cattle from different production systems are not clear."

Study: Reaction of carnosine with aged proteins: another protective process?
"Cellular aging is often associated with an increase in protein carbonyl groups arising from oxidation- and glycation-related phenomena and suppressed proteasome activity. These "aged" polypeptides may either be degraded by 20S proteasomes or cross-link to form structures intractable to proteolysis and inhibitory to proteasome activity. Carnosine (beta-alanyl-l-histidine) is present at surprisingly high levels (up to 20 mM) in muscle and nervous tissues in many animals, especially long-lived species. Carnosine can delay senescence in cultured human fibroblasts and reverse the senescent phenotype, restoring a more juvenile appearance. As better antioxidants/free-radical scavengers than carnosine do not demonstrate these antisenescent effects, additional properties of carnosine must contribute to its antisenescent activity. Having shown that carnosine can react with protein carbonyls, thereby generating "carnosinylated" polypeptides using model systems, we propose that similar adducts are generated in senescent cells exposed to carnosine. Polypeptide-carnosine adducts have been recently detected in beef products that are relatively rich in carnosine, and carnosine's reaction with carbonyl functions generated during amino acid deamidation has also been described. Growth of cultured human fibroblasts with carnosine stimulated proteolysis of long-labeled proteins as the cells approached their "Hayflick limit," consistent with the idea that carnosine ameliorates the senescence-associated proteolytic decline. We also find that carnosine suppresses induction of heme-oxygenase-1 activity following exposure of human endothelial cells to a glycated protein. The antisenescent activity of the spin-trap agent alpha-phenyl-N-t-butylnitrone (PBN) towards cultured human fibroblasts resides in N-t-butyl-hydroxylamine, its hydrolysis product. As hydroxylamines are reactive towards aldehydes and ketones, the antisenescent activity of N-t-butyl-hydroxylamine and other hydroxylamines may be mediated, at least in part, by reactivity towards macromolecular carbonyls, analogous to that proposed for carnosine."

Study: Cooking temperature effects on the forms of iron and levels of several other compounds in beef semitendinosus muscle
"The influence of final cooked temperature on the form of iron present and on the concentration of taurine, carnosine, coenzyme Q10 and creatine was investigated in surface and inner parts of 30-mm thick steaks from beef semitendinosus muscle (n=6). The use of a fast, dry-heat cooking method with a Silex clam cooker (set at 200 °C) led to cooking times ranging from 5.6 to 8.6 min for final internal temperatures of 60 and 85 °C, respectively. The proportion of iron as soluble haem iron decreased from 65% in uncooked meat to 22% when cooked to 60 °C and then decreased more gradually with increases in final cooked temperature. The proportion of insoluble haem iron increased in a reciprocal manner, while changes in the proportions of soluble and insoluble non-haem iron were relatively small, but increases in the percentage of insoluble non-haem iron with increasing final temperature were significant (P<0.01). Changes in the forms of iron with cooking generally took place more rapidly in surface samples than inner samples. On a dry-matter basis, concentrations of taurine, carnosine, coenzyme Q10, and creatine all decreased with cooking, but the decreases were greatest for taurine and creatine. Losses of creatine were at least partly due to conversion to creatinine, and, along with the other compounds, probably included some loss in cooking juices. It is concluded that despite these changes with cooking, beef semitendinosus muscle remains a good source of iron and a useful source of the potentially bioactive compounds taurine, carnosine, coenzyme Q10 and creatine."

Study: Inhibition of Low-Density Lipoprotein Oxidation by Carnosine and Histidine
"Carnosine is a β-alanylhistidine dipeptide found in skeletal muscle and nervous tissue that has been reported to possess antioxidant activity. Carnosine is a potential dietary antioxidant because it is absorbed into plasma intact. This research investigated the ability of carnosine to inhibit the oxidation of low-density lipoprotein (LDL) in comparison to its constituent amino acid, histidine. Carnosine (3 μM) inhibited Cu2+-promoted LDL (20 μg of protein/mL) oxidation at carnosine/copper ratios as low as 1:1, as determined by loss of tryptophan fluorescence and formation of conjugated dienes. Carnosine (6 μM) lost its ability to inhibit conjugated diene formation and tryptophan oxidation after 2 and 4 h of incubation, respectively, of LDL with 3 μM Cu2+. Compared to controls, histidine (3 μM) inhibited tryptophan oxidation and conjugated diene formation 36 and 58%, respectively, compared to 21 and 0% for carnosine (3 μM) after 3 h of oxidation. Histidine was more effective at inhibiting copper-promoted formation of carbonyls on bovine serum albumin than carnosine, but carnosine was more effective at inhibiting copper-induced ascorbic acid oxidation than histidine. Neither carnosine nor histidine was a strong inhibitor of 2,2‘-azobis(2-amidinopropane) dihydrochloride-promoted oxidation of LDL, indicating that their main antioxidant mechanism is through copper chelation."

Study: Effect of dietary carnosine on plasma and tissue antioxidant concentrations and on lipid oxidation in rat skeletal muscle
"The effect of dietary carnosine supplementation on plasma and tissue carnosine and α-tocopherol concentrations and on the formation of thiobarbituric acid reactive substances (TBARS) in rat skeletal muscle homo-genates was evaluated. Plasma, heart, liver and hind leg muscle was obtained from rats fed basal semipurified diets or basal diets containing carnosine (0.0875%), α-tocopheryl acetate (50 ppm), or carnosine (0.0875%) plusα-tocopheryl acetate (50 ppm). Dietary carnosine supplementation did not increase carnosine concentrations in heart, liver and skeletal muscle. Dietary supplementation with both carnosine and α-tocopherol increased carnosine concentrations in liver 1.56-, 1.51- and 1.51-fold as compared with diets lacking carnosine, α-tocopherol or both carnosine and α-tocopherol, respectively. Dietary supplementation with both carnosine and α-tocopherol also increased α-tocopherol concentrations in heart and liver 1.38-fold and 1.68-fold, respectively, as compared to supplementation with α-tocopherol alone. Dietary supplementation with carnosine, α-tocopherol or both carnosine and α-tocopherol was effective in decreasing the formation of TBARS in rat skeletal muscle homogenate, with dietary α-tocopherol and α-tocopherol plus carnosine being more effective than dietary carnosine alone. The data suggest that dietary supplementation with carnosine and α-tocopherol modulates some tissue carnosine and α-tocopherol concentrations and the formation of TBARS in rat skeletal muscle homogenates."

Study: Antioxidative activity of carnosine in gamma irradiated ground beef and beef patties
"The activity of carnosine as a natural antioxidant in gamma irradiated ground beef and beef patties was studied. Samples of ground beef, in the absence and presence of 0.5% or 1.0% carnosine, as well as raw and cooked beef patties prepared with 1.5% salt (NaCl), in the absence and presence of 0.5% or 1.0% carnosine, were gamma irradiated at doses of 0, 2, and 4 kGy. The extent of oxidation in irradiated and non-irradiated samples of ground beef and raw beef patties was then determined during refrigerated (4 ± 1 °C) and frozen (−18 °C) storage, while determined for cooked beef patties during refrigerated storage only. Moreover, the determination of metmyoglobin (MetMb) accumulation and sensory evaluation for the visual color were carried out for samples of ground beef and raw patties. The results indicated that salt or salt and cooking accelerated the oxidative processes and significantly increased the peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) in the prepared non-irradiated samples. However, salt slowed down the accumulation of MetMb in raw patties. Irradiation treatments and storage in the absence of carnosine significantly (P < 0.05) increased the PV and TBARS in samples, at higher rates in salted or salted and cooked beef. Moreover, irradiation and storage significantly (P < 0.05) increased the formation of MetMb in ground beef and raw patties in the absence of carnosine. Addition of carnosine significantly (P < 0.05) reduced the oxidative processes and MetMb formation (proportionally to the used concentration) in samples post-irradiation and during storage. Furthermore, carnosine exerted significant efficacy in maintaining an acceptable visual red color post-irradiation and during storage of ground beef and raw patties. These results demonstrate that carnosine can be successfully used as a natural antioxidant to increase the oxidative stability in gamma irradiated raw and cooked meat products."

Study: The effects of a beef and fish meal on plasma amino acids, insulin and glucagon levels
"In vivo studies have reported the effects of various protein meals on pancreatic hormone secretion. The purpose of the present investigation was to compare the plasma insulin, glucagon and amino acid variations in response to a beef or a fish meal with comparable amino acid content. It was found that the plasma insulin levels increased significantly more with the beef steak meal (from 46.2 ± 3.5 to 153.2 ± 12.6 pmol/l) than with the cod fillet (from 47.8 ± 3.1 to 104.2 ± 9.7). The increase in plasma glucagon following the beef meal (from 64.2 ± 8.1 to 139.4 ± 21.9) was not significantly different from that of the fish meal (from 64.2 ± 7.6 to 119.8 ± 17.8). The increase in plasma amino acids was comparable for both meals except for arginine and lysine which were higher with fish feeding and for histidine when beef was fed. The plama levels of histidine were 30 μmol/l compared to 10μmol/l for the fish meal. This difference may be related to the fact that carnosine, a dipeptide composed of histidine and beta-alanine, is found in high concentrations in beef muscles but is relatively absent in cod fillets. Postprandial studies on time-related variations of plasma histidine and on digestibility or rate of absorption of beef and fish meat are needed in order to identify the factor involved in the difference in insulin secretion between these two nutrients."

Study: The Distribution of Carnosine in the Animal Kingdom

My observations: Carnosine exhibits some antioxidant (and glycation inhibiting) effect. Sufficient carnosine bio-availability can be achieved through consumption of beef. Carnosine prevents oxidation in irradiated meat. Carnosine decreases with cooking time and amount of processing. Carnosine varies depending on muscle group (animal activity).

My recommendation, beef is a valuable source of carnosine especially if you cook it at low temperatures and buy free-range / organic.

#2 Sillewater

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Posted 10 December 2009 - 07:44 PM

I've been looking into creatine in cooked meat. It decreased a lot, so maybe we should supplement with that too.

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#3 JLL

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Posted 10 December 2009 - 08:28 PM

Nice job. I also thought this was interesting:

"The proportion of iron as soluble haem iron decreased from 65% in uncooked meat to 22% when cooked to 60 °C and then decreased more gradually with increases in final cooked temperature. "

I think the reduction in haem iron is good news. My iron intake has probably been too high for quite a while now anyway.

#4 Skötkonung

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Posted 14 December 2009 - 08:17 PM

I thought I would add carnitine to the list:

Study: Postmortem Loss of Carnitine from Skeletal Muscle of Pork and Beef
"The carnitine content of beef muscle postmortem was more than twofold higher than the content of pork muscle. For both pork and beef, carnitine was distributed among the fractions, free carnitine ≫ short-chain acylcarnitine > long-chain acylcarnitine concentration. Based on total carnitine content, the only loss of carnitine from pork muscle occurred as a result of cooking. Cooking also reduced total carnitine content of beef muscle. In addition, total carnitine content of the beef steaks was lower after thawing. Time in the retail case did not influence carnitine content."

Study: Changes in l-carnitine content of fish and meat during domestic cooking
"Human adults store around 20 g of l-carnitine. In the human body, l-carnitine is not metabolized but excreted through the kidney. Lost l-carnitine has to be replenished either by a biosynthetic mechanism or by the consumption of foods containing l-carnitine. Today, there is no “official” recommended daily allowance for l-carnitine but the daily need for l-carnitine intake has been estimated in the wide range of 2–12 μmol/day/kg body weight for an adult human. In this study we evaluated the effect of freezing and of different cooking methods on the l-carnitine content of red meat and fish. l-carnitine was abundantly present in all beef products analyzed. The amounts in the various cuts were similar and our data showed that freezing or cooking did not modify l-carnitine content. Salmon contained about 12 times less l-carnitine than beef but except in smoked salmon, cooking or freezing did not alter l-carnitine content. This study confirms the important role that meet products play for providing adequate amount of l-carnitine to the human body."

Study: L-Carnitine inhibits protein glycation in vitro and in vivo: evidence for a role in diabetic management
"Glycation-initiated changes in tissue proteins are suggested to play an important role in the development of diabetes-related pathological changes. The purpose of this study was to examine the anti-glycating effect of L-carnitine (CA) in vivo in the high-fructose diet-fed rat and to determine the potential of CA to inhibit in vitro glycation. Additionally the glucose-disposal efficiency of CA in the rat diaphragm was investigated. High-fructose diet (60 g/100 g diet)-fed rats were treated with CA (300 mg/kg/day i.p.) for 60 days. The effect of CA on glucose, fructose and fructosamine in plasma, methyl glyoxal and glycated haemoglobin in whole blood and skin and tail tendon collagen glycation were determined. The inhibitory effect of CA on the glycation of bovine serum albumin in vitro was compared with that of aminoguanidine (AG), a known antiglycation agent. Glucose utilisation induced by insulin in the control rat diaphragm was monitored in the presence and absence of CA. High-fructose feeding induced hyperglycaemia and glycation of haemoglobin and skin and tail tendon collagen. In CA-administered fructose-fed rats glycation was significantly reduced. In vitro glycation and accumulation of advanced glycation end products were mitigated by CA. CA was more effective than AG in inhibiting glycation in vitro. CA also enhanced the utilisation of glucose in the rat diaphragm. The findings of the study reveal that CA not only has antiglycation effect but also enhances glucose disposal in the rat diaphragm. These findings provide evidence for the therapeutic utility of CA in diabetes and associated complications."

Study: L-carnitine: implications in the treatment of the metabolic syndrome and Type 2 diabetes
"The metabolic syndrome (MS) is a conglomeration of inter-related common clinical disorders, including obesity, glucose intolerance, hypertension and dyslipidemia, which predispose to Type 2 diabetes (T2D) and cardiovascular diseases. Hyperinsulinemia, per se, and insulin resistance are the pathogenic factors associated with the metabolic risk factors. Since these risk factors are the most frequent causes for mortality among patients with T2D and the MS, treatments targeting normalization of both lipid and glucose homeostasis are of interest. The crucial role of L-carnitine (CA) as a regulator of lipid and glucose metabolism has raised considerable interest in its use as a potential tool for therapeutic intervention in the MS. Several clinical studies have, therefore, been undertaken to examine the efficacy and other benefits in the treatment of T2D and the MS. Studies from rodent models of MS have also shown the positive effects of CA on several components of the syndrome. CA, being an endogenous water-soluble nutrient, could be a safe adjunct and a relevant future drug for the MS. This review provides an overview on the importance of CA in T2D and the MS and the need for further evaluation of its inclusion in treatment protocols."

Study: Metabolic Fate of Dietary Carnitine in Human Adults: Identification and Quantification of Urinary and Fecal Metabolites
"Results of kinetic and pharmacokinetic studies have suggested that dietary carnitine is not totally absorbed and is in part degraded in the gastrointestinal tract of humans. To determine the metabolic fate of dietary carnitine in humans, we administered orally a tracer dose of [methyl-3H]L-carnitine with a meal to subjects who had been adapted to a low-carnitine diet or a high-carnitine diet. Urinary and fecal excretion of radiolabeled carnitine and metabolites was monitored for 5 to 11 d following administration of the test dose. Total radioactive metabolites excreted ranged from 13 to 34% (low carnitine diet) and 27 to 46% (high carnitine diet) of the ingested tracer. Major metabolites found were [3H]trimethylamine N-oxide (8 to 39% of the administered dose; excreted primarily in urine) and [3H]{gamma}-butyrobetaine (0.09 to 8% of the administered dose; excreted primarily in feces). Urinary excretion of total carnitine was 42 to 95% (high carnitine diet) and 190 to 364% (low carnitine diet) of intake. These results indicate that oral carnitine is 54 to 87% bioavailable from normal Western diets; the percentage of intake absorbed is related to the quantity ingested."

Study: Species and muscle differences in L-carnitine levels in skeletal muscles based on a new simple assay
"We have adapted the enzymatic method [Biochemical and Biophysical Research Communications 176 (3) (1991) 1617] for the safe and rapid assay of L-carnitine (L-CA) in skeletal muscle using a microplate reader. The concentration of L-CA in fresh semitendinosus muscle from broiler chicken, pig, beef cattle, deer, horse and goat muscle were 0.69, 1.09, 1.86–3.57, 4.57, 4.95 and 11.36 μmol/g wet weight, respectively. The animals which had higher concentration of L-CA, also had the highest amounts of myoglobin as an index to the redness of the muscle. Furthermore, we investigated this relationship between white muscle, M. pectoralis profundus, and red muscle, M. soleus, in laying hens. The L-CA and myoglobin concentration in red muscle were significantly higher than those in white muscle (p<0.01). These findings suggest that L-CA concentration in muscle is related to oxygen metabolism and to myofiber types."

Does a diet low in animal products cause deficiencies in l-carnitine?

Study: Carnitine status of lactoovovegetarians and strict vegetarian adults and children
"Because carnitine is contained primarily in meats and dairy products, vegetarian diets provide a model for assessing the impact of prolonged low carnitine intake on carnitine status. Plasma carnitine concentrations and urinary carnitine excretion were measured in adults and children consuming a strict vegetarian, lactoovovegetarian, or mixed diet. In adults plasma carnitine concentration and urinary carnitine excretion of strict vegetarians and lactoovovegetarians were significantly lower than those in the mixed-diet group but were not different from each other. In children significant differences were found between all three diet groups for both plasma carnitine concentration and urinary carnitine excretion. The differences in plasma carnitine concentrations were greater in children than in adults, possibly reflecting the effects of growth and tissue deposition. Small differences between diet groups in adults do not suggest a nutritionally significant difference in carnitine status. Whether vegetarian children are at greater risk for overt deficiency is not answered. "

Study: Correlation of carnitine levels to methionine and lysine intake.
"Plasma carnitine levels were measured in two alternative nutrition groups--strict vegetarians (vegans) and lactoovovegetarians (vegetarians consuming limited amounts of animal products such as milk products and eggs). The results were compared to an average sample of probands on mixed nutrition (omnivores). Carnitine levels were correlated with the intake of essential amino acids, methionine and lysine (as substrates of its endogenous synthesis), since the intake of carnitine in food is negligible in the alternative nutrition groups (the highest carnitine content is in meat, lower is in milk products, while fruit, cereals and vegetables contain low or no carnitine at all). An average carnitine level in vegans was significantly reduced with hypocarnitinemia present in 52.9% of probands. Similarly, the intake of methionine and lysine was significantly lower in this group due to the exclusive consumption of plant proteins with reduced content of these amino acids. Carnitine level in lactoovovegetarians was also significantly reduced, but the incidence of values below 30 micromol/l was lower than in vegans representing 17.8% vs. 3.3% in omnivores. Intake of methionine and lysine was also significantly reduced in this group, but still higher compared to vegans (73% of protein intake covered by plant proteins). Significant positive correlation of carnitine levels with methionine and lysine intake in alternative nutrition groups indicates that a significant portion of carnitine requirement is covered by endogenous synthesis. Approximately two thirds of carnitine requirement in omnivores comes from exogenous sources. The results demonstrate the risks of alternative nutrition with respect to the intake of essential amino acids, methionine and lysine, and with respect to the intake and biosynthesis of carnitine."

Study: Systemic carnitine deficiency exacerbated by a strict vegetarian diet.
"A 12-year old boy suffered episodes of vomiting, lethargy, and hypoglycaemia from the age of 1 year. Adhering to a vegetarian diet caused an increase in frequency and severity of the attacks. It was found that he was suffering from systemic carnitine deficiency that responded promptly to treatment with L-carnitine."

#5 TheFountain

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Posted 15 December 2009 - 12:22 PM

I've been meaning to work carnosine into my regimen but I haven't gotten around to it yet. I can't seem to found it anywhere for less than about 20$ for a month supply. But i'll keep looking.

Edited by TheFountain, 15 December 2009 - 12:22 PM.


#6 Skötkonung

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Posted 16 December 2009 - 10:03 AM

I've been meaning to work carnosine into my regimen but I haven't gotten around to it yet. I can't seem to found it anywhere for less than about 20$ for a month supply. But i'll keep looking.

Beta alanine may be a solution if l-carnosine is cost prohibitive.

I am looking to completely remove meat from my diet and replace it with this brand of sprouted tofu that I discovered because it can be consumed raw. So far, the reduced meat (and protein) hasn't been detrimental to preserving muscle mass, but my gains have almost completely stopped. I am interested if a higher intake of plant proteins might remedy this issue while maintaining a range of safety. Before completely removing meat, I want to thoroughly assess any benefits it may provide and incorporate them into a supplementation regimen. I have identified a few more compounds and will post in this thread when I have the chance.

My goal is to build a diet that is completely vegetarian and dairy free. Macros will be 50% fat, 15-20% protein, and 30-35% carbohydrate. Everything will be minimally processed or cooked. Fats will be from saturated sources (coconut, dark chocolate) or mono-unsaturated (olive oil). The diet will be low in fructose. It will feature a diverse array of peppers, leafy greens, berries, nuts, seeds, fruits, and sprouted legumes. No gluten or grains. In other words, more or less a carefully engineered vegetarian version of the Paleo diet.

Edited by Skotkonung, 16 December 2009 - 10:06 AM.


#7 Blue

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Posted 16 December 2009 - 10:15 AM

Creatinine may possibly be pro-AGEPs.
http://www.imminst.o...o...st&p=353814

Edited by Blue, 16 December 2009 - 10:20 AM.


#8 TheFountain

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Posted 16 December 2009 - 10:51 AM

I've been meaning to work carnosine into my regimen but I haven't gotten around to it yet. I can't seem to found it anywhere for less than about 20$ for a month supply. But i'll keep looking.

Beta alanine may be a solution if l-carnosine is cost prohibitive.

I am looking to completely remove meat from my diet and replace it with this brand of sprouted tofu that I discovered because it can be consumed raw. So far, the reduced meat (and protein) hasn't been detrimental to preserving muscle mass, but my gains have almost completely stopped. I am interested if a higher intake of plant proteins might remedy this issue while maintaining a range of safety. Before completely removing meat, I want to thoroughly assess any benefits it may provide and incorporate them into a supplementation regimen. I have identified a few more compounds and will post in this thread when I have the chance.

My goal is to build a diet that is completely vegetarian and dairy free. Macros will be 50% fat, 15-20% protein, and 30-35% carbohydrate. Everything will be minimally processed or cooked. Fats will be from saturated sources (coconut, dark chocolate) or mono-unsaturated (olive oil). The diet will be low in fructose. It will feature a diverse array of peppers, leafy greens, berries, nuts, seeds, fruits, and sprouted legumes. No gluten or grains. In other words, more or less a carefully engineered vegetarian version of the Paleo diet.


Are you making this move to compare your biomarkers on this vegetarian version of the Paleo diet with the ordinary paleo diet? I would be very interested in seeing what your IFG-1 figures look like after a month or two on this diet. Essentially you would be consuming the same type of diet I do, which is a cross-combination of raw food vegetarian/paleo. One thing I still consume, as I mentioned to you in our private message correspondences, is eggs. But I make a very conscious decision to only consume organic Omega 3 eggs. I have been considering re-incorporating a small amount of soy into my diet for hormonal balance purposes. But I need to assess the necessity of this. This might sound weird but when dairy is excluded from my diet I notice that thyroid symptoms seem to disappear and that my thyroid gland seems less swollen. I will look into beta alanine and whatever relevant studies on glycation there are.

Edited by TheFountain, 16 December 2009 - 10:53 AM.


#9 Sillewater

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Posted 16 December 2009 - 11:06 AM

I've been meaning to work carnosine into my regimen but I haven't gotten around to it yet. I can't seem to found it anywhere for less than about 20$ for a month supply. But i'll keep looking.

Beta alanine may be a solution if l-carnosine is cost prohibitive.

I am looking to completely remove meat from my diet and replace it with this brand of sprouted tofu that I discovered because it can be consumed raw. So far, the reduced meat (and protein) hasn't been detrimental to preserving muscle mass, but my gains have almost completely stopped. I am interested if a higher intake of plant proteins might remedy this issue while maintaining a range of safety. Before completely removing meat, I want to thoroughly assess any benefits it may provide and incorporate them into a supplementation regimen. I have identified a few more compounds and will post in this thread when I have the chance.

My goal is to build a diet that is completely vegetarian and dairy free. Macros will be 50% fat, 15-20% protein, and 30-35% carbohydrate. Everything will be minimally processed or cooked. Fats will be from saturated sources (coconut, dark chocolate) or mono-unsaturated (olive oil). The diet will be low in fructose. It will feature a diverse array of peppers, leafy greens, berries, nuts, seeds, fruits, and sprouted legumes. No gluten or grains. In other words, more or less a carefully engineered vegetarian version of the Paleo diet.


I've been wondering about sprouted soy products. Are they safe? Especially with the trypsin inhibitors.

According to this paper 7 days of sprouting is still not deemed safe:

http://www.sproutnet...utrient_and.pdf

and according to this one, in vitro digestibility was still not improved with germination:

Effect of Sprouting on invitro digestibility of some locally consumed leguminous seeds.

While this paper suggests that it is the chemical form of the soy protein that is important.

http://www.aaccnet.o...1995/72_401.pdf

I have read through some papers in the past and recent studies seem to support the idea that sprouting decreases Trypsin Inhibitors, but I have not seen any that showed improved digestibility. And also, are the isoflavones from soy actually healthy? Could you post some studies on their health benefits? \

You've probably researched it thoroughly and I would just like your opinion.

Looking forward to future posts on some of the beneficial components of meat.

Edited by Sillewater, 16 December 2009 - 11:08 AM.


#10 Skötkonung

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Posted 16 December 2009 - 10:10 PM

I've been wondering about sprouted soy products. Are they safe? Especially with the trypsin inhibitors.

According to this paper 7 days of sprouting is still not deemed safe:

http://www.sproutnet...utrient_and.pdf

and according to this one, in vitro digestibility was still not improved with germination:

Effect of Sprouting on invitro digestibility of some locally consumed leguminous seeds.

While this paper suggests that it is the chemical form of the soy protein that is important.

http://www.aaccnet.o...1995/72_401.pdf

I have read through some papers in the past and recent studies seem to support the idea that sprouting decreases Trypsin Inhibitors, but I have not seen any that showed improved digestibility. And also, are the isoflavones from soy actually healthy? Could you post some studies on their health benefits?

You've probably researched it thoroughly and I would just like your opinion.

Looking forward to future posts on some of the beneficial components of meat.

This is the tofu product that I consume (VacPack Tofu Super Firm):
http://www.pulmuonew...d.com/plain.asp

That is an excellent point about the amount of time required to reduce trypsin inhibitors content. The packaging on the product makes no mention of the sprouting process, so I contacted their customer service representatives via email. Hopefully I will have an answer for you soon.

Soy is an incomparable gas producer. Accordingly, research dollars have poured into studies with titles such as "Flavor and flatulence factors in soybean protein products," "Effects of various soybean products on flatulence in the adult man," "Development of a technique for the in vivo assessment of flatulence in dogs" and so forth. Studies comparing types of soyfoods (tempeh, tofu, soy protein isolate, etc.) and/or different strains of soybeans (hybrid or genetically engineered) in terms of their flatulence potential are commonplace.

It is my understanding that flatulence with soy and other legume products has a primary causes: oligosaccharides.

The best known oligosaccharides in beans are raffinose and stachyose. They require the enzyme alpha-galactosidase to be digested properly. Unfortunately, humans and other mammals do not come so equipped. Fortunately, this is not the primary issue with tofu, as carbohydrate is mostly processed out of the final product [source], [source], and [source]. Carbohydrate in soy generally constitute 30 percent of the bean and break down into soluble sugars of sucrose (5 percent), stachyose (4 percent), raffinose (1 percent) and insoluble fiber (20 percent). Unlike other beans, soybean carbohydrate contains very little starch (which humans can digest) - less than 1 percent. Neither home cooking nor high-temperature industrial heating processes dispatch raffinose and stachyose. However, germination, which occurs during the fermentation process, will dramatically reduce the amount of these sugars, with a complete disappearance of the oligosaccharides on the third day [source].. Incubation with microrganisms or enzymes derived from microorganisms also has this good effect.

Imbalances in gut flora caused by trypsin inhibitors (which inhibit protein digestion) may be part of the problem, though undigested protein itself is not. Circulating levels of insulin, gastrin, gastric inhibitory polypeptide, pancreatic polypeptide and neurotensin are affected by trypsin inhibitors, but do not seem involved in flatulent dyspepsia [source].

In my anecdotal experience, consuming sprouted tofu has not caused any gas. :-D The sprouting process must be working in that regard. But how has it affected the trypsin inhibitor content and do trypsin inhibitors really pose a risk to proper nutrition? Well, since trypsin inhibitor content has also been correlated to issues with digestion, I would expect any significant quantity to also cause me gas.

Researchers in France found that a 3 day germination process reduced trypsin inhibitor activity in raw soybeans by 30 percent while increasing vitamin C content [source], and that the results grow proportionately to germination time. Another in vitro study found that a 51.68% reduction in trypsin inhibitor activity was achieved through sprouting [source]. Other studies show similar results [source].

Without knowing the duration of sprouting and temperature that occurs with the Wildwood product I discussed earlier, I cannot speculate as to what extent trypsin inhibitor activity is deactivated. However, since the fermented soybeans are processed to remove excess carbohydrate and fat before being emulsified into tofu, much the trypsin inhibitor content is likely also removed with the bean waste.

The bottom line is that if one is alternating soy products with other sources of protein, it shouldn't cause any issue. Given the long history of soy consumption in Asia and the apparent lack of consequence on total lifespan and healthspan, I conclude that soy consumption (non-GMO, sprouted) is neutral at worst.

Furthermore, isoflavones may have some beneficial properties:

Link: Antioxidant and antipromotional effects of the soybean isoflavone genistein.
Link: Genistein, daidzein, and their .beta.-glycoside conjugates: antitumor isoflavones in soybean foods from American and Asian diets
Link: Dietary Isoflavones: Biological Effects and Relevance to Human Health
Link: Antioxidant Activity of Phytoestrogenic Isoflavones
Link: Antioxidant mechanisms of isoflavones in lipid systems: paradoxical effects of peroxyl radical scavenging
Link: Antioxidant Activities of Isoflavones and Their Biological Metabolites in a Liposomal System
Link: Isoflavone phytoestrogens consumed in soy decrease F2-isoprostane concentrations and increase resistance of low-density lipoprotein to oxidation in humans1

Edited by Skotkonung, 16 December 2009 - 10:12 PM.


#11 Skötkonung

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Posted 16 December 2009 - 11:40 PM

Sillewater, before I jump off the deep end and join the soy eating groupies, I thought I might see if Loren Cordain has any input beyond what has already been discussed. Sure enough, he does:

"Tofu and tempeh are sources of soy bean agglutinin (SBA). SBA has harmful properties because they break cell membranes. This can induce increased intestinal permeability, which is associated to certain autoimmune diseases and low-grade inflammation. SBA has also been shown to stimulate the immune system, something we don't want in an inflammatory disease."

WHFoods does a decent job covering the topic:
http://www.whfoods.c...d...ip&dbid=292

I am now wondering if I should act to reduce soy and find another protein source. Perhaps just stick to red meat :-D I'll be honest with you, protein source is where I am really struggling right now.

Edited by Skotkonung, 16 December 2009 - 11:41 PM.


#12 Sillewater

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Posted 17 December 2009 - 05:56 AM

I agree, finding a good protein source is hard. The majority of my protein is from seafood and red meat. 1/4 from vegetarian protein powder.

#13 sentrysnipe

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Posted 17 December 2009 - 06:23 AM

genistein will give you boobies, stunt your growth, and crank down your ft4 levels (eventually hypothyroidism), probably why most asian males have feminized features (round face - estrogen, short stature, etc.) through years of soy as a staple.

some people say only eat fermented soy (to avoid IP6, oxalate calcification) but I say down with any soy entirely! :-D

maybe in moderation, but not as a regular food.

#14 PerfectSeek

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Posted 17 December 2009 - 01:31 PM

I think trying to find a vegetarian/supplement to replace meat is idealistic, and probably impossible. But let us know if you find something that works... I'd be impressed.

Edited by PerfectSeek, 17 December 2009 - 01:31 PM.


#15 sentrysnipe

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Posted 17 December 2009 - 11:44 PM

mushroom has high protein for a vegetable, has a slightly meaty texture too. i like it.

#16 EmbraceUnity

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Posted 19 December 2009 - 08:02 AM

Besides the typical veggie proteins: soy, beans, nuts, seeds, and wheat gluten, there is also: quinoa, hemp, chickpeas, rice protein, and pea protein.

In Vitro Meat seems to be progressing nicely, and should theoretically allow any nutrient ratios that one desires, but it isn't available to consumers yet, and early reports claim it is "soggy."

Sentrysnipe,

Mycoprotein is a similar concept, and it is a complete protein, but the only consumer source I know of is Quorn brand products. Though those use egg and milk as binding agents. Mycoprotein is derived from fungus. Would love to purchase it in bulk powder form.

Edited by progressive, 19 December 2009 - 08:44 AM.





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