Mala B. Rao
National Chemical Laboratory
9 Papers
182 Citations
Mala B. Rao is an academic researcher from National Chemical Laboratory. The author has contributed to research in topics: Fermentation & Proteases. The author has an hindex of 7, co-authored 9 publications.
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Papers
Molecular and Biotechnological Aspects of Microbial Proteases
TL;DR: Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes and deciphering these secrets would enable to exploit proteases for their applications in biotechnology.
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Molecular and industrial aspects of glucose isomerase.
TL;DR: Manipulation of the GI gene by site-directed mutagenesis holds promise that a GI suitable for biotechnological applications will be produced in the foreseeable future.
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Optimization and scale up of production of alkaline protease from Conidiobolus coronatus
R. Seeta Laxman,Atul P. Sonawane,Snehal Vijay More,B. Seetarama Rao,Meenakshi V. Rele,Vittal V. Jogdand,Vasanti Deshpande,Mala B. Rao +7 more
TL;DR: Optimization of fermentation conditions in shake flasks and scale up of production to 100 L in fermentors and preservation and stabilization studies showed that glycerol conferred considerable stabilization at room temperature while ammonium sulphate precipitated enzyme at 0.9 saturation was best with stability up to 2 years even at roomTemperature.
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Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20)
TL;DR: The effect of a wide variety of compounds was studied to enhance the thermal stability of the protease by modification of its microenvironment and addition of Ca2+ or glycine was effective in increasing the half-life of the enzyme three-fold.
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Induction and catabolite repression of cellulase inPenicillium funiculosum
TL;DR: Both endoglucanase and xylan enzyme activity were induced by CMC, whereas xylan induced only xylanase activity, and the effect of protease on induction of cellulase activity is discussed.
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