Stable earthworm serine proteases: Application of the protease function and usefulness of the earthworm autolysate
Stable earthworm serine proteases: Application of the protease function and usefulness of the earthworm autolysate
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DOI:
10.1016/s1389-1723(00)80106-1
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发表时间:
2000-08-01
影响因子:
2.8
通讯作者:
Ishihara, K
中科院分区:
文献类型:
--
作者:
Nakajima, N;Sugimoto, M;Ishihara, K
The fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N. et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993), 60, 293-300 (1996), and 63, 2031-2033 (1999)] were further characterized to exploit their catalytic functions. These enzymes are stable in solution for long periods at room temperature and strongly resistant to organic solvents, even toluene and n-hexane. The serine proteases can act on various protein substrates such as elastin and hemoglobin as well as fibrin, and also catalyzed the hydrolysis of esters such as ethyl acetate and a bioplastic, poly[(R)-3-hydroxybutyrate] film. The enzymes, In the absence of microbial degradation, contributed to the production of the earthworm autolysate possessing antioxidant ability and protease activity, whose components were similar to those of soy sauce. The extract of the earthworm autolysate could be used as a peptone substitute in media for the cultivation of microorganisms.