Optimal immobilization of β-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using response surface methodology and its applications

被引:78
作者
Dwevedi, Alka [1 ]
Kayastha, Arvind M. [1 ]
机构
[1] Banaras Hindu Univ, Sch Biotechnol, Fac Sci, Varanasi 221005, Uttar Pradesh, India
关键词
beta-Galactosidase; Sephadex; Chitosan; Immobilization; Lactose hydrolysis; PACKED-BED REACTOR; LACTOSE HYDROLYSIS; IN-VITRO; OPTIMIZATION; STABILITY; BACTERIA; ENZYMES; UREASE; SYSTEM; MEDIA;
D O I
10.1016/j.biortech.2008.12.048
中图分类号
S2 [农业工程];
学科分类号
082806 [农业信息与电气工程];
摘要
Response surface methodology (RSM) and centre composite design (CCD) were used to optimize immobilization of beta-galactosidase (BGAL) from Pisum sativum onto two matrices: Sephadex G-75 and chitosan beads. The immobilization efficiency of 75.66% and 75.19% were achieved with Sephadex G-75 and chitosan, respectively. There was broad divergence in physico-chemical properties of Sephadex-PsBGAL and chitosan-PsBGAL Chitosan-PsBGAL was better suited for industrial application based on its broad pH and temperature optima, higher temperature stability, reusability etc. Sephadex-PsBGAL and chitosan-PsBGAL showed much variation in their catalytic properties with respect to soluble enzyme. About 50% loss in activity of Sephadex-PsBGAL and chitosan-PsBGAL were observed after 12 and 46 days at 4 degrees C, respectively. Chitosan-PsBGAL showed higher rate of lactose hydrolysis present in milk and whey at room temperature and 4 degrees C than Sephadex-PsBGAL. In both cases, lactose of milk whey was hydrolyzed at higher rate than that of milk. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2667 / 2675
页数:9
相关论文
共 30 条
[1]
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[2]
Stability and catalytic kinetics of acid phosphatase immobilized on composite beads of chitosan and activated clay [J].
Chang, MY ;
Juang, RS .
PROCESS BIOCHEMISTRY, 2004, 39 (09) :1087-1091
[3]
Optimization of media composition for Nattokinase production by Bacillus subtilis using response surface methodology [J].
Deepak, V. ;
Kalishwaralal, K. ;
Ramkumarpandian, S. ;
Babu, S. Venkatesh ;
Senthilkumar, S. R. ;
Sangiliyandi, G. .
BIORESOURCE TECHNOLOGY, 2008, 99 (17) :8170-8174
[4]
Dey P. M., 1984, ADV ENZYMOLOGY RELAT, V56, P180
[5]
Haaland P.D., 1989, EXPT DESIGN BIOTECHN, P61
[6]
JOUENNE T, 1994, FEMS MICROBIOL LETT, V119, P237
[7]
SPECIFICITY OF GLUCOSE OXIDASE (NOTATIN) [J].
KEILIN, D ;
HARTREE, EF .
BIOCHEMICAL JOURNAL, 1952, 50 (03) :331-341
[8]
ENTRAPMENT OF PROTEINS BY AGGREGATION WITHIN SEPHADEX BEADS [J].
KHARE, SK ;
VAIDYA, S ;
GUPTA, MN .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 1991, 27 (03) :205-216
[9]
KOSARIC N, 1985, ADV BIOCHEM ENG, V19, P25
[10]
KRAJEWSKA B, 1990, J CHEM TECHNOL BIOT, V48, P337