ISSN: 0256-1115 (print version) ISSN: 1975-7220 (electronic version)
Copyright © 2024 KICHE. All rights reserved

Articles & Issues

Language
English
Conflict of Interest
In relation to this article, we declare that there is no conflict of interest.
Publication history
Received October 2, 2007
Accepted November 30, 2007
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Copyright © KIChE. All rights reserved.

All issues

Immobilization of α-amylase from Bacillus licheniformis on developed support using microbial transglutaminase

1Department of Bioscience and Biotechnology, College of Engineering, Silla University, Gwaebop-dong 1-1, Busan 617-736, Korea 2Department of Pharmaceutical Engineering, College of Medical Life Science, Silla University, Gwaebop-dong 1-1, Busan 617-736, Korea
jhalee@silla.ac.kr
Korean Journal of Chemical Engineering, July 2008, 25(4), 801-803(3), 10.1007/s11814-008-0131-1
downloadDownload PDF

Abstract

α-amylase from Bacillus licheniformis was successfully immobilized on developed support, which was prepared by coating a chitosan-casein film on silica, at 20 ℃, pH 6.0 for 5 hr with microbial transglutaminase (MTG) as the cross-linking factor. The optimal support was obtained when 1% chitosan and 1% casein were used in the coating mixture. The optimal condition for immobilization catalyzed by MTG was confined to be at MTG concentration of 15 U/mL, pH 6.0, reacting for 6 hr at 20 ℃. The highest specific activity of immobilized α-amylase was achieved as 236 U/g. After immobilization, the obtained enzyme showed broader pH profile and maintained more than 70% of the original activity after 20 reuses.

References

Kim DJ, Shin DH, Hur BK, Kim EK, J. Microbiol. Biotechnol., 6, 836 (2000)
Aksoy S, Tumturk H, Hasirci N, J. Biotechnol., 60, 37 (1998)
Mutry VR, Bhat J, Muniswaran PKA, Biotrchnol. Bioprogress Eng., 7, 57 (2002)
Lee SK, Park SW, Kim YI, Chung KH, Hong SI, Kim SW, Korean J. Chem. Eng., 19(2), 261 (2002)
Zheng LY, Xiao YL, Korean J. Chem. Eng., 21(1), 201 (2004)
Tominaga J, Kamiya N, Doi S, Ichinose H, Maruyama T, Goto M, Biomacromolecules, 6(4), 2299 (2005)
Synowiecki J, Wolosowska S, Enzyme Microb. Technol., 39(7), 1417 (2006)
Faergemand M, Murray BS, Dickinson E, Qvist KB, Int. Dairy J., 9, 343 (1999)
Mariniello L, Porta R, Prog. Exp. Tum. Res., 38, 174 (2005)
Dincer A, Telefoncu A, J. Mol. Catal. B-Enzym., 45, 10 (2007)
Kim TY, Cho SY, Korean J. Chem. Eng., 22(5), 691 (2005)
lkram-ul-Haq, Ashraf H, Qadeer MA, Iqbal J, Bioresour. Technol., 96(10), 1201 (2005)
Joshi S, Yadav S, Nerurkar A, Desai AJ, J. Microbiol. Biotechnol., 2, 313 (2007)
Zhu Y, Rinzema A, Tramper J, Bol J, Biotechnol. Bioeng., 50(3), 291 (1996)
Grossowicz N, Wainfan E, Borek E, Waelsch H, J. Biol. Chem., 187, 111 (1950)
Rick W, Stegbauer HP, Methods of enzymatic analysis, Weinheim, Verlag-Chemie, Germany (1974)
Xi FN, Wu JM, J. Chromatogr., 1057, 41 (2004)
Bayramoglu G, Yilmaz M, Arica MY, Food Chem., 84, 591 (2004)
Kara A, Yavuz BH, Besirli N, Denizli A, React. Funct. Polym., 62, 61 (2005)
Kang SC, Kim HJ, Nam SW, Oh DK, J. Microbiol. Biotechnol., 5, 766 (2002)

The Korean Institute of Chemical Engineers. F5, 119, Anam-ro, Seongbuk-gu, 233 Spring Street Seoul 02856, South Korea.
TEL. No. +82-2-458-3078FAX No. +82-507-804-0669E-mail : kiche@kiche.or.kr

Copyright (C) KICHE.all rights reserved.

- Korean Journal of Chemical Engineering 상단으로