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来自嗜碱芽孢杆菌的两种耐热碱性木聚糖酶的纯化及性质

Purification and properties of two thermostable alkaline xylanases from an alkaliphilic bacillus sp.

作者信息

Gessesse A

机构信息

Department of Biology, Addis Ababa University, Addis Ababa, Ethiopia.

出版信息

Appl Environ Microbiol. 1998 Sep;64(9):3533-5. doi: 10.1128/AEM.64.9.3533-3535.1998.

DOI:10.1128/AEM.64.9.3533-3535.1998
PMID:9726912
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC106762/
Abstract

Two xylanases, designated XylA and XylB, were purified from the culture supernatant of the alkaliphilic Bacillus sp. strain AR-009. The molecular masses of the two enzymes were estimated to be 23 kDa (XylA) and 48 kDa (XylB) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pHs for activity were 9 for XylA and 9 to 10 for XylB. The temperature optima for the activity of XylA were 60 degreesC at pH 9 and 70 degreesC at pH 8. XylB was optimally active at 75 degreesC at pH 9 and 70 degreesC at pH 8. Both enzymes were stable in a broad pH range and showed good stability when incubated at 60 and 65 degreesC in pH 8 and 9 buffers.

摘要

从嗜碱芽孢杆菌AR-009菌株的培养上清液中纯化出两种木聚糖酶，分别命名为XylA和XylB。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计这两种酶的分子量分别为23 kDa（XylA）和48 kDa（XylB）。XylA的最佳活性pH值为9，XylB的最佳活性pH值为9至10。XylA在pH 9时活性的最佳温度为60℃，在pH 8时为70℃。XylB在pH 9时于75℃活性最佳，在pH 8时于70℃活性最佳。两种酶在较宽的pH范围内都很稳定，并且当在pH 8和9的缓冲液中于60℃和65℃孵育时表现出良好的稳定性。

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