Amazoniac
Member
For those who have struggled with gelatin or even hydrolyzed collagen in the past, this study might offer some clues regarding fermentation of cartilage from connective tissue. Also, how having poor metabolism and gut health can trigger present infections by adding fermentable substrate.
I don't know if pressure cooking is enough to breakdown those compounds but simmering for a long time is probably not (add to that the issue with glutamates, etc).
http://dspace.library.uu.nl/bitstream/h ... 012-46.pdf
"Crude protein [in feces] was greatest (P < 0.05) for collagen, followed by rabbit hair, casein, rabbit skin, and chicken (Gallus gallus domesticus) cartilage. Moderate amounts of CP were found in glucosamine-chondroitin, glucosamine, and rabbit bone, whereas CP was not detected in the FOS and cellulose substrates."
Which indicates undigested (and with greater chances of being fermented)?
"Nitrogen-free extract was greatest in FOS, high in glucosamine-chondroitin and glucosamine, moderate in cartilage, and low in all other substrates."
Does this indicates protein utilization?
"The greatest total SCFA production was recorded for FOS (P < 0.05), followed by collagen, casein, and glucosamine (P < 0.05). The FOS and collagen showed comparable acetate production. [highlight=yellow]Collagen not only had a high production of total SCFA but also resulted in a greater acetate to propionate ratio relative to all other substrates[/highlight] (8.41:1 for collagen and 1.67:1−2.97:1 for other substrates). Chicken cartilage and glucosamine-chondroitin produced similar total SCFA production, which was moderate compared with FOS (P < 0.05)."
"As far as we know, the present study showed for the fi rst time that specifi c components in animal tissues have the ability to contribute to intestinal microbial fermentation in the cheetah, and most probably in other felids as well."
"[...]As such, our fi ndings indicated the need to account for fermentable compounds from animal origin in the diet of carnivores and may provide new insights into promoting intestinal health."
"Type 1 collagen is present in bone tissues, tendons, ligaments, and skin, and is the most abundant collagen in the body (Asghar and Henrickson, 1982). Collagen differs from most proteins as it is a complex mesh of fibrils, which are essentially compact molecular clumps. Although collagen is generally regarded as a protein, it is known that glucose and galactose are covalently bound and form an integral part of the collagen protein structure in vertebrate tissues (Asghar and Henrickson, 1982). Moreover, connective tissue contains substantial concentrations of glycosaminoglycans, especially cartilage. Connective tissue may, therefore, make an important contribution to the carbohydrate fraction of the diet of a carnivore besides hepatic glycogen. [highlight=yellow]If not digested enzymatically in the small intestine, these compounds will provide protein and carbohydrate substrates to the large intestinal microbiota.[/highlight]"
"Although only moderate in its NFE [lacking nitrogen] content, chicken cartilage resulted in the greatest Rmax [rate of gas production] value, which was achieved in a relatively short period of time (Tmax = 1.2 h). This indicates that specific bacteria, capable of utilizing cartilage components in a more efficient manner than other substrates, were present in the inoculum insufficient concentration to elicit almost immediate fermentation."
"Animal-derived substrates low in carbohydrates and OMCV also showed considerable SCFA production. Despite the absence of NFE, concentrations of total SCFA for collagen were second greatest of all tested substrates, indicating that substantial fermentation took place."
"Taking gas production kinetics as well as SCFA production into account, glucosamine and chondroitin sulfate were highly fermentable, whereas casein, chicken cartilage, and collagen were only moderately fermentable compared with the positive control (FOS)."
"Although protein fermentation also produces acetate, butyrate, and to a lesser extent, propionate (Macfarlane et al., 1992), the branched-chain fatty acids, as part of the intestinal SCFA, mainly originate from protein fermentation (Rasmussen et al., 1988)."
I don't know if pressure cooking is enough to breakdown those compounds but simmering for a long time is probably not (add to that the issue with glutamates, etc).
http://dspace.library.uu.nl/bitstream/h ... 012-46.pdf
"Crude protein [in feces] was greatest (P < 0.05) for collagen, followed by rabbit hair, casein, rabbit skin, and chicken (Gallus gallus domesticus) cartilage. Moderate amounts of CP were found in glucosamine-chondroitin, glucosamine, and rabbit bone, whereas CP was not detected in the FOS and cellulose substrates."
Which indicates undigested (and with greater chances of being fermented)?
"Nitrogen-free extract was greatest in FOS, high in glucosamine-chondroitin and glucosamine, moderate in cartilage, and low in all other substrates."
Does this indicates protein utilization?
"The greatest total SCFA production was recorded for FOS (P < 0.05), followed by collagen, casein, and glucosamine (P < 0.05). The FOS and collagen showed comparable acetate production. [highlight=yellow]Collagen not only had a high production of total SCFA but also resulted in a greater acetate to propionate ratio relative to all other substrates[/highlight] (8.41:1 for collagen and 1.67:1−2.97:1 for other substrates). Chicken cartilage and glucosamine-chondroitin produced similar total SCFA production, which was moderate compared with FOS (P < 0.05)."
"As far as we know, the present study showed for the fi rst time that specifi c components in animal tissues have the ability to contribute to intestinal microbial fermentation in the cheetah, and most probably in other felids as well."
"[...]As such, our fi ndings indicated the need to account for fermentable compounds from animal origin in the diet of carnivores and may provide new insights into promoting intestinal health."
"Type 1 collagen is present in bone tissues, tendons, ligaments, and skin, and is the most abundant collagen in the body (Asghar and Henrickson, 1982). Collagen differs from most proteins as it is a complex mesh of fibrils, which are essentially compact molecular clumps. Although collagen is generally regarded as a protein, it is known that glucose and galactose are covalently bound and form an integral part of the collagen protein structure in vertebrate tissues (Asghar and Henrickson, 1982). Moreover, connective tissue contains substantial concentrations of glycosaminoglycans, especially cartilage. Connective tissue may, therefore, make an important contribution to the carbohydrate fraction of the diet of a carnivore besides hepatic glycogen. [highlight=yellow]If not digested enzymatically in the small intestine, these compounds will provide protein and carbohydrate substrates to the large intestinal microbiota.[/highlight]"
"Although only moderate in its NFE [lacking nitrogen] content, chicken cartilage resulted in the greatest Rmax [rate of gas production] value, which was achieved in a relatively short period of time (Tmax = 1.2 h). This indicates that specific bacteria, capable of utilizing cartilage components in a more efficient manner than other substrates, were present in the inoculum insufficient concentration to elicit almost immediate fermentation."
"Animal-derived substrates low in carbohydrates and OMCV also showed considerable SCFA production. Despite the absence of NFE, concentrations of total SCFA for collagen were second greatest of all tested substrates, indicating that substantial fermentation took place."
"Taking gas production kinetics as well as SCFA production into account, glucosamine and chondroitin sulfate were highly fermentable, whereas casein, chicken cartilage, and collagen were only moderately fermentable compared with the positive control (FOS)."
"Although protein fermentation also produces acetate, butyrate, and to a lesser extent, propionate (Macfarlane et al., 1992), the branched-chain fatty acids, as part of the intestinal SCFA, mainly originate from protein fermentation (Rasmussen et al., 1988)."