意大利青霉果胶裂解酶的纯化及某些性质

Purification and some properties of the pectin lyase from Penicillium italicum.

作者信息

Alaña A, Lama M J, Serra J L

机构信息

Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad del País Vasco/Euskal Herriko Unibertsitatea, Bilbao, Spain.

出版信息

FEBS Lett. 1991 Mar 25;280(2):335-40. doi: 10.1016/0014-5793(91)80325-w.

DOI:10.1016/0014-5793(91)80325-w

PMID:2013333

Abstract

For the first time, a pectin lyase (poly(methoxygalacturonide)lyase: EC 4.2.2.10) from a member of the generus Penicillium was isolated, purified to homogeneity and characterized. The monomeric enzyme from Penicillium italicum CECT 2294 culture filtrates showed a molecular mass of 34 kDa after SDS-electrophoresis in polyacrylamide gradient gels, and the isoelectric point was 8.6 as determined by isoelectric focusing. The optimum pH (9.0), the high pH and temperature stabilities, the ability to degrade pectins from different sources and with a wide range of degrees of esterification (from 37% to 86%) as well as the importance of this type of biocatalysts in the food industry make this enzyme an interesting subject of study.

摘要

首次从青霉属的一个成员中分离出一种果胶裂解酶（聚（甲氧基半乳糖醛酸）裂解酶：EC 4.2.2.10），将其纯化至同质并进行了表征。意大利青霉CECT 2294培养滤液中的单体酶在聚丙烯酰胺梯度凝胶中进行SDS电泳后显示分子量为34 kDa，通过等电聚焦测定其等电点为8.6。该酶的最佳pH值（9.0）、高pH值和温度稳定性、降解不同来源且具有广泛酯化度（37%至86%）果胶的能力以及这类生物催化剂在食品工业中的重要性，使其成为一个有趣的研究对象。