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
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
收藏
页码:2800 / 2805
页数:6
相关论文
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