Abstract
SUMMARYBeef round muscle was separated according to solubility characteristics into water soluble, salt soluble and insoluble fractions. These showed different degrees of hydrolysis when reacted with an enzyme. The magnitude varied with nature of the enzyme. Collagenase, bromelain and trypsin showed stronger solubilizing activity on the insoluble fraction than on the salt soluble fraction; whereas papain, Rhozyme P‐11 and ficin showed strong activity on the salt soluble fraction and hydrolyzed the insoluble fraction less efficiently. In general, the water soluble fraction was more resistant to enzyme hydrolysis than the other fractions, except with papain and Rhozyme P‐11. However, the portion of the water soluble fraction, that was hydrolyzed appeared as smaller peptides than the solubilized fregments of the other two fractions.
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