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Purification and characterization of a thermostable endo-β-1,4-glucanase by a novel strain of Penicillium purpurogenum

Authors
 Kyoung-Mi Lee  ;  Marimuthu Jeya  ;  Ah-Reum Joo  ;  Raushan Singh  ;  In-Won Kim  ;  Jung-Kul Lee 
Citation
 ENZYME AND MICROBIAL TECHNOLOGY, Vol.46(3-4) : 206-211, 2010 
Journal Title
 ENZYME AND MICROBIAL TECHNOLOGY 
ISSN
 0141-0229 
Issue Date
2010
Keywords
Catalytic efficiency ; Endo-β-1,4-glucanase ; Penicillium purpurogenum ; Thermostability
Abstract
A novel endo-β-1,4-glucanase (EG)-producing strain was isolated and identified as Penicillium purpurogenum KJS506 based on its morphology and internal transcribed spacer (ITS) rDNA gene sequence. P. purpurogenum produced one of the highest levels of EG (5.6 U mg-protein−1) with rice straw and corn steep powder as carbon and nitrogen sources, respectively. The extracellular EG was purified to homogeneity by sequential chromatography of P. purpurogenum culture supernatants on a DEAE sepharose column, a gel filtration column, and then on a Mono Q column with fast protein liquid chromatography. The purified EG was a monomeric protein with a molecular weight of 37 kDa and showed broad substrate specificity with maximum activity towards lichenan. P. purpurogenum EG showed t1/2 value of 2 h at 70 °C and catalytic efficiency of 118 ml mg−1 s−1, one of the highest levels seen for EG-producing microorganisms. Although EGs have been reported elsewhere, the high catalytic efficiency and thermostability distinguish P. purpurogenum EG.
Full Text
https://www.sciencedirect.com/science/article/pii/S0141022909002555
DOI
10.1016/j.enzmictec.2009.11.002
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Lee, Kyoung Mi(이경미) ORCID logo https://orcid.org/0000-0002-9038-8162
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/158131
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