Journal ArticleDOI
Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit.
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TLDR
The enzyme poorly hydrolyzed triacylglycerols containing n-3 polyunsaturated fatty acids, and appeared as a suitable biocatalyst for selective esterification of sardine free fatty acids with hexanol as substrate, showed a good stability in organic solvents and especially in long chain-fatty alcohol.About:
This article is published in Enzyme and Microbial Technology.The article was published on 2000-03-01. It has received 300 citations till now. The article focuses on the topics: Lipase & Triacylglycerol lipase.read more
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Production, purification, characterization, and applications of lipases.
TL;DR: The production, recovery, and use of microbial lipases are discussed; issues of enzyme kinetics, thermostability, and bioactivity are addressed; and production of recombinant lipases is detailed.
Journal ArticleDOI
Developments in industrially important thermostable enzymes: a review.
TL;DR: The source microorganisms and properties of thermostable starch hydrolysing amylases, xylanases, cellulases, chitinases, proteases, lipases and DNA polymerases are discussed and the industrial needs for such specific thermostably enzyme and improvements required to maximize their application in the future are suggested.
Journal ArticleDOI
Organic solvent-tolerant enzymes
Noriyuki Doukyu,Hiroyasu Ogino +1 more
TL;DR: Most enzymes used in these studies did not originally exhibit high activity and stability in the presence of organic solvents because they were not screened as organic solvent-tolerant enzymes, so their potential for applications in industrial chemical processes is underestimated.
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Enzymatic biodiesel: Challenges and opportunities
TL;DR: A thorough analysis of recent biotechnological progress is presented in the context of present technological challenges and future developmental opportunities aimed at bringing the enzyme costs down and improving the overall process economics towards large scale production of enzymatic biodiesel.
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[Organic solvent-tolerant enzymes].
TL;DR: The use of organic solvents as reaction media for enzymatic reactions provides numerous industrially attractive advantages compared to traditional aqueous reaction systems as mentioned in this paper, however, despite the advantages, native enzymes almost universally exhibit low activities and/or stabilities in the presence of organic solvent-tolerant enzymes.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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Colorimetric Method for Determination of Sugars and Related Substances
TL;DR: In this article, a method was developed to determine submicro amounts of sugars and related substances using a phenol-sulfuric acid reaction, which is useful for the determination of the composition of polysaccharides and their methyl derivatives.
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Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
TL;DR: Small amounts of myoglobin, beta-lactoglobulin, and other proteins and peptides can be spotted or electroblotted onto polyvinylidene difluoride membranes, stained with Coomassie Blue, and sequenced directly, suggesting that PVDF membranes are superior supports for sequence analysis of picomole quantities of proteins purified by gel electrophoresis.