A Study of Purification Profile and Molecular Weight of Fish Visceral Protease Precipitated With Different Precipitating Agents

dc.categoryJournal Article
dc.contributor.authorAnitha Subash
dc.date.accessioned2017-03-09T19:03:50Z
dc.date.available2017-03-09T19:03:50Z
dc.date.issued2014
dc.departmentBiochemistryen_US
dc.description.abstractThe study was aimed at managing the vast amounts of wastes of the redfish Lutjanus sebea to isolate an industrially useful enzyme-protease. The visceral organ waste.s of fish were collected, homogenized with Tris-HCI buffer and precipitated with varying concentrations of ammonium sulphate, aeetone and ethanol and was then purified by dialysis and Sephadex G-lOO column chromatography. The purification profile (the protein content, protease activity, specific activity, purification fold, and recovery %) were studied in the crude and partially purified samples. The results .showed that the activity was maximum when precipitated with 40-60% ammonium sulphate, 100% acetone and 40% ethanol. The fractions with the highest specific activity were selected for further purification by dialysis and Sephadex G-lOO column chromatography. The molecular weight of the isolated enzyme was determined by SDS-PAGE and Native PAGE and was to he found 27 kDa. The presence of protease was confirmed by zymography.en_US
dc.identifier.urihttps://ir.avinuty.ac.in/handle/avu/2055
dc.langEnglishen_US
dc.publisher.nameInternational Journal of Current Researchen_US
dc.publisher.typeInternationalen_US
dc.titleA Study of Purification Profile and Molecular Weight of Fish Visceral Protease Precipitated With Different Precipitating Agentsen_US
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