Author
S.G. Prapulla
Bio: S.G. Prapulla is an academic researcher from Central Food Technological Research Institute. The author has contributed to research in topics: Isoamyl alcohol & Lipase. The author has an hindex of 6, co-authored 6 publications receiving 482 citations.
Papers
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TL;DR: The effects of important reaction parameters for enhancing isoamyl acetate formation through lipase-catalyzed esterification ofisoamyl alcohol were investigated and the operational stability of lipase was also observed to be reasonably high enabling ten reuses of the biocatalyst.
236 citations
TL;DR: A second order response function was developed based on Box-Behnken design of experiments, which indicated optimum conditions for maximum esterification and increased with both E/S ratio and time and decreased with alcohol (acid) concentration.
109 citations
TL;DR: The study demonstrates the potential role of ultrasonication in efficient release of the intracellular FTase which can be used for the production of FOS, an industrially important prebiotic.
51 citations
TL;DR: A rapid and sensitive method has been developed for the estimation of intracellular lipids accumulated in oleaginous yeast cells and a close agreement has been obtained in terms of the values predicted using this relationship.
43 citations
TL;DR: Isoamyl butyrate, an important fruity flavor ester, was synthesized using Rhizomucor miehei lipase immobilized on a weak anion exchange resin (Lipozyme IM-20) by the esterification of isoamyl alcohol and butyric acid by investigating the effects of various reaction parameters.
Abstract: Isoamyl butyrate, an important fruity flavor ester, was synthesized using Rhizomucor miehei lipase immobilized on a weak anion exchange resin (Lipozyme IM-20) by the esterification of isoamyl alcohol and butyric acid. The effects of various reaction parameters such as substrate and enzyme concentrations, substrate molar ratio, temperature and incubation time have been investigated. Yields above 90% were obtained with substrate concentrations as high as 2.0 M. No evidence of enzyme inhibition by butyric acid was present up to 1.0 M concentration. Acid inhibition and, to a small extent, alcohol inhibition were evident above 1.0 M substrate concentration. Conversions reached a saturation value by the end of 24–48 h of incubation due to the accumulation of the water of reaction. The equilibrium was successfully pushed forward towards esterification by removing the accumulated water using a molecular sieve.Journal of Industrial Microbiology & Biotechnology (2000) 25, 147–154.
35 citations
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TL;DR: This review attempts to recast the known information on specificity of lipases in the context of enzyme promiscuity and the beneficial consequences of this promiscuous behavior in biotechnology sectors are discussed.
453 citations
TL;DR: Based on the content of free fatty acids and phosphorus, lipids accumulated from sewage sludge could serve as a substrate for the production of biodiesel.
386 citations
TL;DR: This review examines aspects of oleaginous yeasts not covered in depth in other recent reviews, and proposes standardized terms for units that describe yeast cell mass and lipid production.
380 citations
TL;DR: The present review describes the advantages of lipase-catalyzed reactions in organic Solvents and various effects of organic solvents on their activity.
Abstract: Lipases are industrial biocatalysts, which are involved in several novel reactions, occurring in aqueous medium as well as non-aqueous medium. Furthermore, they are well-known for their remarkable ability to carry out a wide variety of chemo-, regio- and enantio-selective transformations. Lipases have been gained attention worldwide by organic chemists due to their general ease of handling, broad substrate tolerance, high stability towards temperatures and solvents and convenient commercial availability. Most of the synthetic reactions on industrial scale are carried out in organic solvents because of the easy solubility of non-polar compounds. The effect of organic system on their stability and activity may determine the biocatalysis pace. Because of worldwide use of lipases, there is a need to understand the mechanisms behind the lipase-catalyzed reactions in organic solvents. The unique interfacial activation of lipases has always fascinated enzymologists and recently, biophysicists and crystallographers have made progress in understanding the structure-function relationships of these enzymes. The present review describes the advantages of lipase-catalyzed reactions in organic solvents and various effects of organic solvents on their activity.
348 citations
TL;DR: The compiled evidence of high pressure enzyme enhancement indicates that pressure is an effective reaction parameter with potential for greater utilization in enzyme catalysis.
342 citations