Extracellular beta-Glucosidase production by marine Aspergillus sydowii BTMFS 55

The beta-glucosidase enzyme purified from the marine fungus, Aspergillus sydowii BTMFS 55 showed a good yield of enzyme production under solid state fermentation. The statistical optimization of the media components revealed that moisture content, concentration of peptone and inoculum are the major parameters which supported the maximal enzyme production. The purified enzyme showed low pH activity and stability, glucose tolerance and activation by ethanol. It could produce ethanol from wheat bran and rice straw by simultaneous saccharification and fermentation with yeast.The glucosidase purified from Aspergillus sydowii BTMFS 55 shows great potential for several biotechnological applications such as the production of bio-ethanol from agricultural biomass and improvement in the aromatic character of wines and fruit juices through the hydrolysis of flavour glucosidic precursors. There is immense scope for the application of this marine fungus in the biofuel production besides in other industries provided further studies are pursued in exploiting this enzyme and the organism particularly scale up studies with respect to application. There is also ample scope for cloning of the gene encoding beta-glucosidase in domesticated hosts such as Pichia pastoris or S. cerevisiae that can produce ethanol directly from cellulosic biomass.

Extracellular β-glucosidase Production by a Marine Aspergillus sydowii BTMFS 55 under Solid State Fermentation Using Statistical Experimental Design

A potential fungal strain producing extracellular β-glucosidase enzyme was isolated from sea water and identified as ^ëéÉêJ Öáääìë=ëóÇçïáá BTMFS 55 by a molecular approach based on 28S rDNA sequence homology which showed 93% identity with already reported sequences of ^ëéÉêÖáääìë=ëóÇçïáá in the GenBank. A sequential optimization strategy was used to enhance the production of β-glucosidase under solid state fermentation (SSF) with wheat bran (WB) as the growth medium. The two-level Plackett-Burman (PB) design was implemented to screen medium components that influence β-glucosidase production and among the 11 variables, moisture content, inoculums, and peptone were identified as the most significant factors for β-glucosidase production. The enzyme was purified by (NH4)2SO4 precipitation followed by ion exchange chromatography on DEAE sepharose. The enzyme was a monomeric protein with a molecular weight of ~95 kDa as determined by SDS-PAGE. It was optimally active at pH 5.0 and 50°C. It showed high affinity towards éNPG and enzyme has a hã and sã~ñ of 0.67 mM and 83.3 U/mL, respectively. The enzyme was tolerant to glucose inhibition with a há of 17 mM. Low concentration of alcohols (10%), especially ethanol, could activate the enzyme. A considerable level of ethanol could produce from wheat bran and rice straw after 48 and 24 h, respectively, with the help of p~ÅÅÜ~êçãóÅÉë=ÅÉêÉîáëá~É in presence of cellulase and the purified β-glucosidase of ^ëéÉêÖáääìë=ëóÇçïáá BTMFS 55.