Studies of optimum conditions for covalent immobilization of Candida rugosa lipase on poly(γ-glutamic acid) by RSM

被引：75

作者：

Chang, S. -W. ^{[2
]}

Shaw, J. -F. ^{[3
,4
]}

Yang, K. -H. ^{[5
]}

Chang, S. -F. ^{[1
]}

Shieh, C. -J. ^{[1
]}

机构：

[1] Dayeh Univ, Dept Bioind Technol, Da Tsuen, Chang Hua, Taiwan

[2] Chung Chou Univ Technol, Dept Nutr & Hlth Sci, Yuanlin 503, Chang Hua, Taiwan

[3] Natl Chung Hsing Univ, Dept Food Sci & Biotechnol, Taichung 402, Taiwan

[4] Acad Sinica, Inst Plant & Microbial Biol, Taipei 115, Taiwan

[5] Vedan Enterprise Corp Shalu, Taichung 433, Taiwan

来源：

BIORESOURCE TECHNOLOGY | 2008年 / 99卷 / 08期

关键词：

Candida rugosa lipase; covalent binding; immobilization; optimization; poly(gamma-glutamic acid);

D O I：

10.1016/j.biortech.2007.06.020

中图分类号：

S2 [农业工程];

学科分类号：

0828 ;

摘要：

Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on,gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6 h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3 h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein. (c) 2007 Elsevier Ltd. All rights reserved.

引用

页码：2800 / 2805

页数：6

共 25 条

[1] Preparation and characterization of biodegradable nanoparticles based on poly(γ-glutamic acid) with L-phenylalanine as a protein carrier [J].

Akagi, T ;

Kaneko, T ;

Kida, T ;

Akashi, M .

JOURNAL OF CONTROLLED RELEASE, 2005, 108 (2-3) :226-236

[2] Multifunctional conjugation of proteins on/into bio-nanoparticles prepared by amphiphilic poly(γ-glutamic acid) [J].

Akagi, Takami ;

Kaneko, Tatsuo ;

Kida, Toshiyuki ;

Akashi, Mitsuru .

JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION, 2006, 17 (08) :875-892

[3] Reversible immobilization of lipase on phenylalanine containing hydrogel membranes [J].

Arica, MY ;

Kaçar, Y ;

Ergene, A ;

Denizli, A .

PROCESS BIOCHEMISTRY, 2001, 36 (8-9) :847-854

[4] Covalent immobilization of lipase onto hydrophobic group incorporated poly(2-hydroxyethyl methacrylate) based hydrophilic membrane matrix [J].

Bayramoglu, G ;

Kaçar, Y ;

Denizli, A ;

Arica, MY .

JOURNAL OF FOOD ENGINEERING, 2002, 52 (04) :367-374

[5] BIOSYNTHESIS AND CHEMICAL MODIFICATION OF POLY(GAMMA-GLUTAMIC ACID) [J].

BORBELY, M ;

NAGASAKI, Y ;

BORBELY, J ;

FAN, K ;

BHOGLE, A ;

SEVOIAN, M .

POLYMER BULLETIN, 1994, 32 (02) :127-132

[6] Enzyme catalyzed hydrolysis of esters using reversibly soluble polymer conjugated lipases [J].

Charusheela, A ;

Arvind, L .

ENZYME AND MICROBIAL TECHNOLOGY, 2002, 30 (01) :19-25

[7] Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups [J].

Chiou, SH ;

Wu, WT .

BIOMATERIALS, 2004, 25 (02) :197-204

[8] Adsorption immobilization of Candida rugosa lipases on polypropylene hollow fiber microfiltration membranes modified by hydrophobic polypeptides [J].

Deng, HT ;

Xu, ZK ;

Liu, ZM ;

Wu, J ;

Ye, P .

ENZYME AND MICROBIAL TECHNOLOGY, 2004, 35 (05) :437-443

[9]

FUJII H, 1963, J AGR CHEM SOC JPN, V37, P407

[10] Binary immobilization of Candida rugosa lipase on chitosan [J].

Hung, TC ;

Giridhar, R ;

Chiou, SH ;

Wu, WT .

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2003, 26 (1-2) :69-78

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