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 June 23, 2011
Accepted October 24, 2011
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

Production of cellulases and β-glucosidase in Trichoderma reesei mutated by proton beam irradiation

Department of Chemical and Biological Engineering, Korea University, 1, Anam-dong, Sungbuk-gu, Seoul 136-701, Korea 1Center for Environmental Technology Research, Korea Institute of Science and Technology, Seoul 136-130, Korea
kimsw@korea.ac.kr
Korean Journal of Chemical Engineering, July 2012, 29(7), 925-930(6), 10.1007/s11814-011-0272-5
downloadDownload PDF

Abstract

To obtain mutant strains producing high levels of cellulases (FPase and CMCase) and β-glucosidase, Trichoderma reesei KCTC 6950 was mutated by proton beam irradiation. Five mutants were selected out of 1,000 mutants of T.reesei treated with proton beam irradiation, based on their ability for enzyme production on a plate screening medium. In submerged cultures containing Mandel’s fermentation medium, the mutant strain T-2 (MT-2) demonstrated a 165% increase in the activity of FPase, a 146% increase in the activity of CMCase, and a 313% increase in the activity of β-glucosidase, compared with the wild type strain. Additionally, the properties of high level β-glucosidase produced by MT-2 were the same as those of the wild type strain, e.g., an optimum pH of 4.8, and an optimum temperature of 65 ℃. Moreover, the protein concentrations of β-glucosidase produced by the wild type strain and MT-2 were measured by SDS-PAGE, and then β-glucosidase activities were detected by the MUG-zymogram assay.

References

He J, Yu B, Zhang K, Ding X, Chen D, Indian J. Microbiol., 49, 188 (2009)
Bahia A, Ali G, Biochem. Eng. J., 32, 191 (2006)
Wu JC, Ng KR, Chong J, Yang KJ, Lam XP, Nam CT, Nugroho AJ, Korean J. Chem. Eng., 27(2), 469 (2010)
Wang T, Liu X, Yu Q, Zhang X, Qu Y, Gao P, Wang T, Biomol.Eng., 22, 89 (2005)
Gong CS, Ladisch MR, Taso GT, Biotechnol. Bioeng., 19, 959 (1977)
Peyman A, Noraini S, Aidil AH, Wan MY, Biotechnol. Bioprocess Eng., 16, 238 (2011)
Xu F, Wang J, Chen S, Qin W, Yu Z, Zhao H, Xing X, Li H, Appl. Biochem. Microbiol., 47, 53 (2011)
Zhang YHP, Himmel ME, Mielenz JR, Biotechnol. Adv., 24, 452 (2006)
Henrissat B, Driguez H, Viet C, Schulein M, Nat. Biotechnol., 3, 781 (1985)
Gritzali M, Brown RD, Adv. Chem. Ser., 191, 237 (1979)
Ike M, Park J, Tabuse M, Tokuyasu K, Appl. Microbiol. Biotechnol., 87(6), 2059 (2010)
Xiao ZZ, Zhang X, Gregg DJ, Saddler JN, AAPG Bull., 113, 1115 (2004)
Chirico WJ, Brown RD, European J. Biochem., 165, 333 (1987)
Saunders G, Allsop A, Holt G, J. Chem. Technol. Biotechnol., 32, 354 (1882)
Kwon HJ, Park YJ, Yoo YB, Park SY, Kong WS, J.Microbiol. Biotechnol., 17, 1041 (2007)
Kim SB, Kim JS, Lee JH, Kang SW, Park CH, Kim SW, Appl. Biochem. Biotechnol., DOI: 10.1007/s2010-011-9204-4 (2011)
Mandels M, Hontz I, Nystrom J, Biotechnol. Bioeng., 16, 1471 (1974)
Kasana RC, Salwan R, Dhar H, Dutt S, Gulati A, Curr. Microbiol., 57(5), 503 (2008)
Mandels M, Weber J, Adv. Cem. Ser., 95, 391 (1969)
Ghose TK, Appl. Chem., 59, 257 (1987)
Bradford MM, Anal. Biochem., 72, 248 (1976)
Laemmli UK, Nature., 227, 680 (1970)
Lacks SA, Springhorn SS, J. Biol. Chem., 10, 7467 (1980)
Amouri B, Gargouri A, J. Biochem. Eng., 32, 191 (2006)
Farshad D, Jacqueline D, Iraj M, Philippe T, Hamid ZE, New Biotechnol., DOI: 10.1016/ j.nbt.2011.02.002 (2011)
Solov’eva IV, Okunev ON, Vel’kov VV, Koshelev AV, Bubnova TV, Kondrat’eva EG, Skomarovskii AA, Sinitsyn AP, J. Microbiol.
Zaldivar J, Nielsen J, Olsson L, Appl. Microbiol. Biotechnol., 56(1-2), 17 (2001)
He Q, Li N, Chen X, Ye Q, Bai J, Xiong J, Ying H, Korean J. Chem. Eng., 28, 544 (2011)
Allen AL, Roche CD, Biotechnol. Bioeng., 33, 650 (1989)
Gadgil NJ, Daginawala HF, Chakrabarti T, Khanna P, Enzyme Microb. Technol., 17(10), 942 (1995)

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