Abstract
Hydrolysates were prepared from bovine lung, bovine rumen and from partially defatted tissue by treatment at 50°C with either pepsin at pH 3·0, papain at pH 5·5, neutrase at pH 7·0 or alcalase at pH 8·5. For all substrates papain was the most effective hydrolysing agent of those studied whilst neutrase was the least effective. Yields of soluble hydrolysate were high with 45–85 % of the protein being solubilised. In addition, the tissue is, to some extent, defatted during hydrolysis. All enzymes, with the exception of alcalase, readily solubilised the collagen of heated by-products although undenatured (unheated) collagen was, to some extent, resistant to enzymic digestion. Amino acid analysis of the soluble hydrolysates indicated that there was no major loss of any amino acid following prolonged enzymic hydrolysis. In addition, no increase in tyramine concentration occurred during hydrolysis.
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