Abstract
Trypsins from the pyloric caeca of menhaden (Brevoortia spp.) and croaker (Micropogonias furnieri) were used for hydrolysis of both myofibrillar and sarcoplasmic fractions from menhaden muscle. Digestion of muscle proteins was carried out at 37C for 20 min with the pH maintained at either 3, 4, 5, 6, 7, 8 or 9; or for 60 min at the pH's of 5, 7, 8 or 9 at 30C and 37C. The hydrolytic action was evaluated based on the concentration of peptides solubilized. Solubility after digestion of myofibrillar, sarcoplasmic fraction and hemoglobin was optimum at basic pH. The sarcoplasmic fraction was solubilized more than the myofibrillar fraction by both fish trypsins. Similar results were obtained with both crude pyloric extracts and purified trypsins from menhaden and white croaker. Thus, the preparation of the crude pyloric caeca may be preferentially used, because of its low cost as well as the simplicity of the preparative procedure.
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