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Three-phase partitioning of protease from Calotropis procera latex

Paper ID Volume ID Publish Year Pages File Format Full-Text
3856 194 2010 5 PDF Available
Title
Three-phase partitioning of protease from Calotropis procera latex
Abstract

Three-phase partitioning (TPP) was used to partially purify protease from the latex of Calotropis procera (C. procera). To optimize the TPP for protease isolation a ratio of crude extract to t-butanol, percent saturation of (NH4)2SO4, and the cycle of TPP was required. The highest proteolytic recovery (first cycle) of 182% with a purification of 0.95 folds was obtained at the interphase of the system comprising the ratio of the crude extract to t-butanol of 1.0:0.5 with the presence of 50% (NH4)2SO4. The second cycle of TPP was prepared by adding of (NH4)2SO4 up to 65% (w/v) to the bottom phase obtained from 30% (NH4)2SO4–1.0:0.5 system of the first TPP. A purification of 6.92-fold was achieved with about 132% activity recovery. SDS-PAGE and zymography profiles revealed the substantial isolation of protease from C. procera latex by the TPP. The molecular weight of major protease was found to be around 28 kDa. The present study shows high interesting outcomes and could be used as a primary purification process in comparison with existing literature's values.

Keywords
Calotropis procera; Latex; Protease; Three-phase partitioning; t-Butanol
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Three-phase partitioning of protease from Calotropis procera latex
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 50, Issue 3, 15 July 2010, Pages 145–149
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us