This paper describes an enzymatic method of producing gelatin, a method which consists principally of solubilizing the so-called insoluble collagen fibers with a proteolytic enzyme into the form of monomeric collagen molecules. A proteolytic enzyme with a broad specificity, for example, Pronase (a proteolytic enzyme from
Streptoniyces griseus), very easily hydrolyzes, in the presence of CaCl
2, the specific parts of collagen fibers, in which intra- and inter-molecular crosslinks of collagen exist. Therefore, the solubilized molecules consist mainly of a-chains (a constituent polypeptide chain of a collagen molecule) in the case of calf skin and of α-and only small amounts of β-chains (two a-chains are intra-molecularly crosslinked into a β-chain) even in the case of steer hide. Gelatins, which contain only a few n-chain molecules, can be obtained after desalting and inactivating the enzyme only by the heat denaturation of the collagen molecules.
The gelatins thus prepared are of a single-chain character and have the high rigidity modulus of the gels, low intrinsic viscosities, and a narrow distribution of molecular weight.
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