Biochemical characterization of the cutinases from Thermobifida fusca

被引：75
作者：
Chen, Sheng [2 ]
Su, Lingqia [2 ]
Billig, Susan [3 ]
Zimmermann, Wolfgang [3 ]
Chen, Jian [2 ]
Wu, Jing [1 ,2 ]
机构：
[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Sch Biotechnol, Minist Educ, Wuxi 214122, Jiangsu, Peoples R China
[2] Jiangnan Univ, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Jiangsu, Peoples R China
[3] Univ Leipzig, Inst Biochem, Dept Microbiol & Bioproc Technol, D-04103 Leipzig, Germany
来源：
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2010年 / 63卷 / 3-4期
基金：
中国国家自然科学基金;
关键词：
Thermobifida fusca; Cutinase; Characterization; PURIFICATION; LIPASE; PISI; STABILITY; DEPOLYMERIZATION; CHROMATOGRAPHY; OPTIMIZATION; HYDROLYSIS; STRAIN; ENZYME;
D O I：
10.1016/j.molcatb.2010.01.001
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Thermobifida fusca produces two cutinases which share 93% identity in amino acid sequence. In the present study, we investigated the detailed biochemical properties of T. fusca cutinases for the first time. For a better comparison between bacterial and fungal cutinases, recombinant Fusarium solani pisi cutinase was subjected to the similar analysis. The results showed that both bacterial and fungal cutinases are monomeric proteins in solution. The bacterial cutinases exhibited a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters. In addition, the two isoenzymes of T. fusca and the F. solani pisi cutinase are similar in substrate kinetics, the lack of interfacial activation, and metal ion requirements. However, the T. fusca cutinases showed higher stability in the presence of surfactants and organic solvents. Considering the versatile hydrolytic activity, good tolerance to surfactants, superior stability in organic solvents, and thermostability demonstrated by T. fusca cutinases, they may have promising applications in related industries. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码：121 / 127
页数：7
相关论文
共 31 条
[1]   Bacterial lipolytic enzymes: classification and properties [J].
Arpigny, JL ;
Jaeger, KE .
BIOCHEMICAL JOURNAL, 1999, 343 :177-183
[2]   Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase [J].
Brzozowski, AM ;
Savage, H ;
Verma, CS ;
Turkenburg, JP ;
Lawson, DM ;
Svendsen, A ;
Patkar, S .
BIOCHEMISTRY, 2000, 39 (49) :15071-15082
[3]   Identification and characterization of bacterial cutinase [J].
Chen, Sheng ;
Tong, Xing ;
Woodard, Ronald W. ;
Du, Guocheng ;
Wu, Jing ;
Chen, Jian .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (38) :25854-25862
[4]   DSC studies of Fusarium solani pisi cutinase:: consequences for stability in the presence of surfactants [J].
Creveld, LD ;
Meijberg, W ;
Berendsen, HJC ;
Pepermans, HAM .
BIOPHYSICAL CHEMISTRY, 2001, 92 (1-2) :65-75
[5]   Esterification and transesterification catalysed by cutinase in reverse micelles of CTAB for the synthesis of short chain esters [J].
Cunnah, PJ ;
AiresBarros, MR ;
Cabral, JMS .
BIOCATALYSIS AND BIOTRANSFORMATION, 1996, 14 (02) :125-146
[6]   Potential use of cutinase in enzymatic scouring of cotton fiber cuticle [J].
Degani, O ;
Gepstein, S ;
Dosoretz, CG .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2002, 102 (1-6) :277-289
[7]   Fusarium solani pisi cutinase [J].
Egmond, MR ;
de Vlieg, J .
BIOCHIMIE, 2000, 82 (11) :1015-1021
[8]  
Ferrato F, 1997, METHOD ENZYMOL, V286, P327
[9]   SCREENING OF NONFILAMENTOUS BACTERIA FOR PRODUCTION OF CUTIN-DEGRADING ENZYMES [J].
FETT, WF ;
GERARD, HC ;
MOREAU, RA ;
OSMAN, SF ;
JONES, LE .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1992, 58 (07) :2123-2130
[10]  
Gindro K, 1999, FEMS MICROBIOL LETT, V171, P239, DOI 10.1111/j.1574-6968.1999.tb13438.x
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