Optimization of Medium Components for β-glucosidase Production in Schizophyllum commune KUC9397 and Enzymatic Hydrolysis of Lignocellulosic Biomass

Abstract

Medium components for β-glucosidase (BGL) production in Schizophyllum commune KUC9397 were optimized using a central composite design and response surface methodology. From the various medium components tested, cellulose, soy peptone, and thiamine HCl were selected as the optimal carbon, nitrogen, and vitamin sources, respectively. The highest BGL production was obtained with 2.96% cellulose, 2.30% soy peptone, and 0.11% thiamine HCl. BGL production in the optimized medium was increased 7.2-fold compared to production in an unoptimized medium. Crude enzyme preparation from S. commune KUC9397 was used to saccharify pretreated lignocellulosic biomass. The crude enzyme preparations showed statistically equal saccharification rates as Cellobiase, a commercial BGL. This finding indicates that crude enzymes produced by S. commune KUC9397 have good potential for application in cellulosic biomass conversion systems in place of Cellobiase.

Cost-effective production of cellulose hydrolysing enzymes from Trichoderma sp. RCK65 under SSF and its evaluation in saccharification of cellulosic substrates

“…5d showed that increasing soybean meal increased the b-glucosidase production up to a certain concentration (2.4 g) and remained almost constant thereafter. Our results are in well accordance with the work of Lee et al [29] where they used organic nitrogen source soy peptone 2.3 g giving maximum b-glucosidase activity. The predicted values were in good agreement with the values measured in these experiments, thus justifying the validity of the response model and the necessity for optimization.…”

Comparative analysis of the secretomes of Schizophyllum commune and other wood-decay basidiomycetes during solid-state fermentation reveals its unique lignocellulose-degrading enzyme system

“…Several novel families of enzymes that remove xylan side chains, such as acetyl xylan esterases [ 12 ], glucuronoyl esterases [ 13 ], and α-glucuronidases [ 14 , 15 ] have been identified in the cellulolytic system of S. commune . Among the few studies regarding its polysaccharide hydrolases, a recombinant endoxylanase from S. commune has been reported to exhibit very high level of activity against beechwood xylan [ 16 ], and crude enzymes containing mainly β-glucosidase from this fungal species could saccharify pretreated lignocellulose comparably well with a commercial β-glucosidase [ 17 ]. To date, studies of this species have focused mainly on the mating-type gene function [ 18 , 19 ] and mushroom development [ 20 , 21 ], whereas the lignocellulolytic enzymes produced by S. commune are far less characterized and a comprehensive study on its enzymatic system is still lacked.…”

Production, purification and characterization of an acid/alkali and thermo tolerant cellulase from Schizophyllum commune NAIMCC-F-03379 and its application in hydrolysis of lignocellulosic wastes

“…Schizophyllum commune NAIMCC-F-03379 was able to produce comparatively high titre of cellulase enzymes as compared to previous reports (Lee et al 2014 ) with characteristics of highly thermal and pH stable, low K m (0.0909 mg/mL) and high V max (45.45 μmol/min mg) value. The partially purified enzyme showed stability at a wide range of temperature (25–65 °C) and pH (3–10) with 41% (65 °C) and 51% (pH 9) of relative activity respectively after 24 h of incubation.…”

“…The observed R 2 value was comparable with the earlier reports (Muthuvelayudham and Viruthagiri 2010 ; Wang et al 2011 ; Rajeswari et al 2014 ). The effects of media components and β-glucosidase (BGL) production have also been studied in S. commune KUC9397 by Lee et al ( 2014 ) which resulted in 7.2-fold increase in BGL activity. The requirement for fermentation for S. commune NAIMCC-F-03379 for enhanced cellulase activity is comparable to other cellulolytic microorganisms (Pachauri et al 2016 ; Premalatha et al 2015 ).…”