Biochemical characterization of a lichenase from Penicillium occitanis Pol6 and its potential application in the brewing industry

被引:36
作者
Chaari, Fatma [1 ]
Belghith-Fendri, Lilia [1 ]
Blibech, Monia [1 ]
Driss, Dorra [1 ]
Ellouzi, Soumaya Zaouri [1 ]
Sameh, Maktouf [1 ]
Ellouz-Chaabouni, Semia [1 ,2 ]
机构
[1] Sfax Univ, Sfax Natl Sch Engineers, Dept Biol, Unite Enzymes & Bioconvers, Sfax 3038, Tunisia
[2] Sfax Natl Sch Engineers, Unite Serv Commun Bioreacteur Couple Ultrafiltre, Sfax 3038, Tunisia
关键词
Lichenase; Penicillium occitanis; Brewing industry; BETA-GLUCANASE; BETA-1,3-1,4-GLUCANASE LICHENASE; THERMOSTABLE BETA-1,3-1,4-GLUCANASE; 1,3-1,4-BETA-D-GLUCANASE LICHENASE; TALAROMYCES-EMERSONII; BROILER-CHICKENS; PURIFICATION; GENE; OPTIMIZATION; PERFORMANCE;
D O I
10.1016/j.procbio.2014.02.023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The purification and characterization of an extracellular lichenase from the fungus Penicillium occitanis Pol6 were studied. The strain produced the maximum level of extracellular lichenase (45 +/- 5 U ml(-1)) when grown in a medium containing oat flour (2%, w/v) at 30 degrees C for 7 days. The purified enzyme EG(L) showed as a single protein band on SDS-PAGE with a molecular mass of 20 kDa. Its N-terminal sequence of 10 amino acid residues was determined as LDNGAPLLNV. The purified enzyme showed an optimum activity at pH 3.0 and 50-60 degrees C. The half-lives of EG(L) at 60 degrees C and 70 degrees C were 80 min and 21 min, respectively. Substrate specificity studies revealed that the enzyme is a true beta-1,3-1,4-D-glucanase. The enzyme hydrolyzed lichenan to yield trisaccharide, and tetrasaccharide as the main products. Under simulated mashing conditions, addition of EG(L) (20 U/ml) or a commercial beta-glucanase (20 U/ml) reduced the filtration time (25% and 21.3%, respectively) and viscosity (10% and 8.18%, respectively). These characteristics indicate that EG(L) is a good candidate in the malting and brewing industry. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1040 / 1046
页数:7
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