Effect of Glycosylation and Additional Domains on the Thermostability of a Family 10 Xylanase Produced by Thermopolyspora flexuosa

被引：44

作者：

Anbarasan, Sasikala ^{[1
]}

Janis, Janne ^{[2
]}

Paloheimo, Marja ^{[3
]}

Laitaoja, Mikko ^{[2
]}

Vuolanto, Minna ^{[3
]}

Karimaki, Johanna ^{[1
]}

Vainiotalo, Pirjo ^{[2
]}

Leisola, Matti ^{[1
]}

Turunen, Ossi ^{[1
]}

机构：

[1] Aalto Univ, Dept Biotechnol & Chem Technol, Espoo 02015, Finland

[2] Univ Joensuu, Dept Chem, FIN-80101 Joensuu, Finland

[3] Roal Oy, Rajamaki 05201, Finland

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2010年 / 76卷 / 01期

基金：

芬兰科学院;

关键词：

CARBOHYDRATE-BINDING MODULE; NONOMURAEA-FLEXUOSA; THERMOTOGA-MARITIMA; CATALYTIC-ACTIVITY; STABILITY; INCREASES; CLONING; FUSION; THERMOPHILUM; PURIFICATION;

D O I：

10.1128/AEM.00357-09

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.

引用

页码：356 / 360

页数：5

共 35 条

[1] Importance of the carbohydrate-binding module of Clostridium stercorarium Xyn10B to xylan hydrolysis [J].

Ali, MK ;

Hayashi, H ;

Karita, S ;

Goto, M ;

Kimura, T ;

Sakka, K ;

Ohmiya, K .

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2001, 65 (01) :41-47

[2] The use of forced protein evolution to investigate and improve stability of family 10 xylanases -: The production of Ca2+-independent stable xylanases [J].

Andrews, SR ;

Taylor, EJ ;

Pell, G ;

Vincent, F ;

Ducros, VMA ;

Davies, GJ ;

Lakey, JH ;

Gilbert, HJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (52) :54369-54379

[3] Effect of family 22 carbohydrate-binding module on the thermostability of Xyn10B catalytic module from Clostridium stercorarium [J].

Araki, Rie ;

Karita, Shuichi ;

Tanaka, Akiyoshi ;

Kimura, Tetsuya ;

Sakka, Kazuo .

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2006, 70 (12) :3039-3041

[4] The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling [J].

Arnold, K ;

Bordoli, L ;

Kopp, J ;

Schwede, T .

BIOINFORMATICS, 2006, 22 (02) :195-201

[5] A MODULAR XYLANASE CONTAINING A NOVEL NONCATALYTIC XYLAN-SPECIFIC BINDING DOMAIN [J].

BLACK, GW ;

HAZLEWOOD, GP ;

MILLWARDSADLER, SJ ;

LAURIE, JI ;

GILBERT, HJ .

BIOCHEMICAL JOURNAL, 1995, 307 :191-195

[6] Glycoforms of β-lactoglobulin with improved thermostability and preserved structural packing [J].

Broersen, K ;

Voragen, AGJ ;

Hamer, RJ ;

de Jongh, HHJ .

BIOTECHNOLOGY AND BIOENGINEERING, 2004, 86 (01) :78-87

[7] The X6 "thermostabilizing" domains of xylanases are carbohydrate-binding modules:: Structure and biochemistry of the Clostridium thermocellum X6b domain [J].

Charnock, SJ ;

Bolam, DN ;

Turkenburg, JP ;

Gilbert, HJ ;

Ferreira, LMA ;

Davies, GJ ;

Fontes, CMGA .

BIOCHEMISTRY, 2000, 39 (17) :5013-5021

[8] Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms [J].

Chen, B ;

Bautista, R ;

Yu, K ;

Zapata, GA ;

Mulkerrin, MG ;

Chamow, SM .

PHARMACEUTICAL RESEARCH, 2003, 20 (12) :1952-1960

[9] Recombinant his-tagged DNA polymerase. I. Cloning, purification and partial characterization of Thermus thermophilus recombinant DNA polymerase [J].

Dabrowski, S ;

Kur, J .

ACTA BIOCHIMICA POLONICA, 1998, 45 (03) :653-660

[10] Cloning, expression, and purification of the His6-tagged hyper-thermostable dUTPase from Pyrococcus woesei in Escherichia coli:: application in PCR [J].

Dabrowski, S ;

Ahring, BK .

PROTEIN EXPRESSION AND PURIFICATION, 2003, 31 (01) :72-78

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