来自嗜碱芽孢杆菌菌株（N137）的编码内切-β-1,4-木聚糖酶的基因xyaA的克隆与DNA测序
Cloning and DNA sequencing of xyaA, a gene encoding an endo-beta-1,4-xylanase from an alkalophilic Bacillus strain (N137).
作者信息
Tabernero C, Sánchez-Torres J, Pérez P, Santamaría R I
机构信息
Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas/Universidad de Salmanca, Spain.
出版信息
Appl Environ Microbiol. 1995 Jun;61(6):2420-4. doi: 10.1128/aem.61.6.2420-2424.1995.
Abstract
The gene xyaA encoding an alkaline endo-beta 1,4-xylanase from an alkalophilic Bacillus sp. strain (N137) isolated in our laboratory was cloned and expressed in Escherichia coli. The nucleotide sequence of a 1,656-bp DNA fragment containing xyaA was determined, revealing one open reading frame of 993 bp that encodes a xylanase (XyaA) of 39 kDa. This xylanase lacks a typical putative signal peptide, yet the protein is found in the Bacillus culture supernatant. In Escherichia coli, the active protein is located mainly in the periplasmic space. The xylanase activity of the cloned XyaA is an endo-acting enzyme that shows optimal activity at pH 8 and 40 degrees C. This activity is stable at a pH between 6 and 11. Incubations of XyaA at 40 degrees C for 1 h destroyed 45% of the activity.
摘要
我们实验室分离得到的嗜碱芽孢杆菌菌株（N137）中编码碱性内切-β-1,4-木聚糖酶的基因xyaA被克隆并在大肠杆菌中表达。测定了包含xyaA的1656 bp DNA片段的核苷酸序列，发现一个993 bp的开放阅读框，其编码一个39 kDa的木聚糖酶（XyaA）。该木聚糖酶缺乏典型的假定信号肽，但该蛋白存在于芽孢杆菌培养上清液中。在大肠杆菌中，活性蛋白主要位于周质空间。克隆的XyaA的木聚糖酶活性是一种内切酶，在pH 8和40℃时显示最佳活性。该活性在pH 6至11之间稳定。XyaA在40℃孵育1小时会破坏45%的活性。
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