Abstract
The desulfhydration from l-cysteine in the larvae of the webbing clothes moth, Tineola bisselliella, was mainly due to l-cysteine lyase. The enzyme, which has previously been found only in the yolk sac of the developing chicken embryo, catalyzed β-replacement of l-cysteine, producing H 2S and lanthionine. In the presence of added sulfite, the enzyme catalyzes the formation of H 2S and cysteic acid. To examine the correlation between l-cysteine lyase and keratin digestion by Tineola larvae, two kinds of larval extracts were prepared: one contained protease and l-cysteine lyase; the other contained only protease. The efficiency of keratin degradation with l-cysteine lyase was higher than that without the enzyme.
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