Journal Articles
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Item Microbial production of tannase: State of the art(2011) Belur, P.D.; Mugeraya, G.Tannin acyl hydrolase (E.C.3.1.1.20) is commonly referred as tannase, hydrolyses ester and depside bonds of hydrolysable tannins to produce gallic acid, glucose and galloyl esters. Tannase finds application in many industrial sectors which includes pharmaceutical, food, chemical and beverages industry. The enzyme has potential uses in the treatment of tannery effluents and pre-treatment of tannin containing animal feed. Since, the discovery of tannase in 1867, a great deal of research did happen on production aspects of tannase. Most of the research was focused on fungal tannase, as tannin was earlier considered as bacteriostatic. After the discovery of bacterial tannase in 1983, several studies on bacterial tannase were published. Despite the long history and numerous publications, tannase is still considered as one of the costly industrial enzymes. This is due to less titer and long fermentation time of the processes. In view of the growing demand, it is imperative to isolate high productive strains and develop economically feasible processes. This study reviews the microbial sources, isolation and screening methods, modes of production, substrates and media, temperature and pH of fermentation, duration of fermentation and location of tannase enzyme. An attempt is also made to give an outline of historical development which has taken place in tannase research.© 2011 Academic Journals Inc.Item Utilization of renewable agricultural residues for the production of extracellular halostable cellulase from newly isolated halomonas sp. strain PS47(2013) Shivanand, P.; Mugeraya, G.; Kumar, A.A newly isolated biopolymer-degrading halophilic bacterium, Halomonas sp. strain PS47, yielded higher cellulase activity (0.0076 U/ml) in mineral salt medium (MM63). Activity increased to 0.029 U/ml when carboxymethyl cellulose (0.5 % w/v) was used as carbon source and further to 0.138 U/ml when a combination of yeast extract and peptone was used as nitrogen source. Enzyme secretion was maximal during late exponential and stationary phases (0.15 U/ml, 48 h). Among different agro-residues (1 % w/v), wheat bran gave the highest activity (0.12 U/ml) at pH 7.5, 30 °C and 6 % (w/v) NaCl. The cellulase exhibited higher activity at pH 7.1 and 50 °C. The enzyme exhibited activity over a wide range of NaCl concentrations (0-4 M). Optimum activity was at 0-1 M NaCl. At 4 M NaCl, activity was reduced to 65 % of the initial value. The present investigation thus contributes to the limited information available on halostable cellulases. © Springer-Verlag Berlin Heidelberg and the University of Milan 2012.