Journal ArticleDOI
Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20)
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TLDR
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.About:
This article is published in Enzyme and Microbial Technology.The article was published on 1995-02-01. It has received 97 citations till now. The article focuses on the topics: Conidiobolus coronatus & Protease.read more
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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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Microbial alkaline proteases: From a bioindustrial viewpoint
C. Ganesh Kumar,Hiroshi Takagi +1 more
TL;DR: In this paper, a review of the proteases that can resist extreme alkaline environments produced by a wide range of alkalophilic microorganisms is presented, and various nutritional and environmental parameters affecting the production of alkaline proteases are delineated.
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An overview on fermentation, downstream processing and properties of microbial alkaline proteases
TL;DR: Alkaline proteases useful for detergent applications are mostly active in the pH range 8–12 and at temperatures between 50 and 70°C, with a few exceptions of extreme pH optima up to pH 13 and activity at temperatures up to 80–90°C.
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Thermostable alkaline protease from bacillus brevis and its characterization as a laundry detergent additive
TL;DR: An alkaline protease from a facultatively thermophilic and alkalophilic strain of Bacillus brevis has been studied and it could remove blood stains completely when used with detergents in the presence of Ca2+ and glycine.
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Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11.
TL;DR: The purpose of the research was to study the purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11, which was shown to have a relative low molecular weight and improve the cleansing power of various detergents.
References
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Living with water stress: evolution of osmolyte systems
TL;DR: Osmolyte compatibility is proposed to result from the absence of osmolytes interactions with substrates and cofactors, and the nonperturbing or favorable effects of oSMolytes on macromolecular-solvent interactions.
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Increased thermal stability of proteins in the presence of sugars and polyols
TL;DR: The difference between the partial molar volume of the sugar or polyol and its van der Waals volume was used as a rough quantitative measure of the structure-making or structure-breaking effect.
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Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation
L. J. Perry,Ronald Wetzel +1 more
TL;DR: The cross-linked T4 lysozyme was more stable than the wild type during incubation at elevated temperatures as determined by recovered enzymatic activity at 20 degrees C.
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A new way of enhancing the thermostability of proteases
TL;DR: Surprisingly it is found that a single mutation that decreases thermostability can require two mutations that increase stability to compensate for it, suggesting cooperativity.
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The multicatalytic proteinase of mammalian cells
TL;DR: Inhibition of proteinase activity by thiol reagents supports the suggestion that the enzyme is a cysteineproteinase but there is some evidence that it may be a serine proteinase and the catalytic mechanism is at present unknown.