Purification and biochemical characterization of a novel thermostable lichenase from Aspergillus niger US368

被引：34

作者：

Elgharbi, Fatma ^{[1
]}

Hmida-Sayari, Aida ^{[1
]}

Sahnoun, Mouna ^{[1
]}

Kammoun, Radhouane ^{[1
]}

Jlaeil, Lobna ^{[2
]}

Hassairi, Hajer ^{[2
]}

Bejar, Samir ^{[1
]}

机构：

[1] Univ Sfax, LMB, CBS, Sfax 3018, Tunisia

[2] Univ Sfax, Lab Anal, CBS, Sfax 3018, Tunisia

来源：

CARBOHYDRATE POLYMERS | 2013年 / 98卷 / 01期

关键词：

Aspergillus niger US368; beta-1,3; 1,4-Glucanase; Thermostability; Statistical experimental designs; BETA-GLUCANASES; 1,3-1,4-BETA-D-GLUCANASE LICHENASE; BETA-1,3-1,4-GLUCANASE LICHENASE; TALAROMYCES-EMERSONII; ESCHERICHIA-COLI; BROILER-CHICKENS; GENE; IDENTIFICATION; SUCCINOGENES; PERFORMANCE;

D O I：

10.1016/j.carbpol.2013.07.009

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

New beta-1,3;1,4-glucanase was purified from Aspergillus niger US368. The pure glucanase has a molecular mass of about 32 kDa. The N-terminal sequence of the purified enzyme (A-G-T-N-P-P-I-G-V) was determined. The optimum pH and temperature recorded for enzyme activity were 5 and 60 degrees C, respectively. It also displayed marked thermostability with a half-life of 30 min at 70 degrees C. At 37 degrees C, the enzyme showed 100% stability from pH 3 to 10. The K-m and V-max values exhibited by the enzyme on barley beta-glucan were 0.62 mg ml(-1) and 34.46 U ml(-1), respectively. The enzyme is a retaining-one and was only active toward glucan containing beta-1,3;1,4-linkages. The production of beta-glucanase with barley flour as the sole carbon source was optimized. This is the first report on the purification and characterization of a beta-1,3;1,4-glucanase from A. niger. This lichenase could be considered as a candidate for future application particularly in the animal feed industry. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：967 / 975

页数：9

共 43 条

[1] Isolation and identification of mixed linked β-glucan degrading bacteria in the intestine of broiler chickens and partial characterization of respective 1,3-1,4-β-glucanase activities [J].