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加利福尼亚对虾中肠腺胰凝乳蛋白酶的生化特性研究

Biochemical characterisation of chymotrypsin from the midgut gland of yellowleg shrimp, Penaeus californiensis.

作者信息

Navarrete-del-Toro Maria A, García-Carreño Fernando L, Hernández-Cortés Patricia, Molnár Tamas, Gráf Laszlo

机构信息

Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Calle IPN 195, La Paz, B.C.S. 23090, Mexico.

Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Calle IPN 195, La Paz, B.C.S. 23090, Mexico.

出版信息

Food Chem. 2015 Apr 15;173:147-55. doi: 10.1016/j.foodchem.2014.09.160. Epub 2014 Oct 7.

DOI:10.1016/j.foodchem.2014.09.160
PMID:25466006
Abstract

Chymotrypsin from shrimp, Penaeus californiensis, was compared to Bos taurus chymotrypsin, and its structure-function relationship was studied. Catalytic efficiency toward synthetic substrate is lower, but it has a broad specificity and higher activity toward protein substrates, including collagen. It is active at pH 4-10 and fully active up to 50 °C for 2 h and at least nine days at room temperature. The activation peptide is twice as long as bovine chymotrypsinogen, has less disulfide bridges, and is a single polypeptide. Only one activation step is necessary from chymotrypsinogen to the mature enzyme. Postmortem implications in muscle softening and melanisation, resistance to temperature and pH and efficiency with proteinaceous substrates make chymotrypsin useful as a biotechnological tool in food processing. This makes shrimp processing wastes useful as a material for production of fine reagents.

摘要

对加利福尼亚对虾的胰凝乳蛋白酶与牛胰凝乳蛋白酶进行了比较,并研究了其结构-功能关系。它对合成底物的催化效率较低,但具有广泛的特异性,对包括胶原蛋白在内的蛋白质底物具有更高的活性。它在pH 4-10时具有活性,在50°C下2小时内完全有活性,在室温下至少九天保持活性。激活肽的长度是牛胰凝乳蛋白酶原的两倍,二硫键较少,是一条单一多肽链。从胰凝乳蛋白酶原到成熟酶只需要一步激活。胰凝乳蛋白酶在肌肉软化和黑化、对温度和pH的耐受性以及对蛋白质底物的作用效率方面的死后影响,使其成为食品加工中一种有用的生物技术工具。这使得虾加工废料成为生产精细试剂的有用材料。

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