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在稀释条件下,纤维素酶EC 3.2.1.4对大麦β-葡聚糖的水解作用与大麦可溶酶的水解作用相同。

The hydrolysis of barley beta-glucan by the cellulase EC 3.2.1.4 under dilute conditions is identical to that of barley solubilase.

作者信息

Wilhelmi C, Morgan K

机构信息

Industrial Research Limited, Lower Hutt, New Zealand.

出版信息

Carbohydr Res. 2001 Feb 15;330(3):373-80. doi: 10.1016/s0008-6215(00)00298-6.

Abstract

Barley beta-glucan solubilase is an enzyme that degrades barley beta-glucan in extracts obtained from barley flour. The solubilase preferentially attacks the longer blocks of beta-(1-->4) linkages, i.e., those containing at least nine glucosyl residues. There is strong evidence to suggest that the solubilase derives from fungi associated with the husk of the grain. It was found that cellulase (EC 3.2.1.4) from Trichoderma sp. shows similar activity under dilute conditions. Since fungi associated with the husk of the grain are known to produce these types of cellulases, there is no need, based on current evidence, to propose the existence of a unique enzyme, i.e., solubilase, for the solubilising behaviour of enzymes in the barley grain.

摘要

大麦β-葡聚糖溶解酶是一种能降解从大麦粉中提取的提取物中的大麦β-葡聚糖的酶。该溶解酶优先作用于较长的β-(1→4)键连接片段,即那些含有至少九个葡萄糖基残基的片段。有充分证据表明,该溶解酶源自与谷物外壳相关的真菌。研究发现,来自木霉属的纤维素酶(EC 3.2.1.4)在稀释条件下表现出类似的活性。由于已知与谷物外壳相关的真菌会产生这类纤维素酶,基于目前的证据,无需提出存在一种独特的酶,即溶解酶,来解释大麦籽粒中酶的溶解行为。

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