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Understanding β‐mannanase from Streptomyces sp. CS147 and its potential application in lignocellulose based biorefining
Author(s) -
Yoo Hah Y.,
Pradeep G. C.,
Lee Soo K.,
Park Don H.,
Cho Seung S.,
Choi Yun H.,
Yoo Jin C.,
Kim Seung W.
Publication year - 2015
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201500150
Subject(s) - biorefining , bioconversion , chemistry , cellulase , hydrolysis , biorefinery , enzymatic hydrolysis , substrate (aquarium) , hydrogen peroxide , chromatography , biochemistry , food science , fermentation , organic chemistry , raw material , biology , ecology
Hydrolytic enzymes such as cellulase and hemicellulase have been attracted in lignocellulose based biorefinery. Especially, mannanase has been a growing interest in industrial applications due to its importance in the bioconversion. In this study, an extracellular endo‐β‐1,4‐D‐mannanase was produced by Streptomyces sp. CS147 (Mn147) and purified 8.5‐fold with a 43.4% yield using Sephadex G‐50 column. The characterization of Mn147 was performed, and the results were as follows: molecular weight of ∼25 kDa with an optimum temperature of 50°C and pH of 11.0. The effect of metal ions and various reagents on Mn147 was strongly activated by Ca +2 but inhibited by Mg +2 , Fe +2 , hydrogen peroxide, EDTA and EGTA. K m and V max values of Mn147 were 0.13 mg/mL and 294 μmol/min mg, respectively, when different concentrations (3.1 to 50 mg/mL) of locust bean gum galactomannan were used as substrate. In enzymatic hydrolysis of heterogeneous substrate (spent coffee grounds), Mn147 shows a similar conversion compared to commercial enzymes. In addition, lignocellulosic biomass can be hydrolyzed to oligosaccharides (reducing sugars), which can be further utilized for the production of biomaterials. These results showed that Mn147 is attractive in quest of potential bioindustrial applications.