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Purification and properties of an extracellular cold-active protease from the psychrophilic bacterium Pseudoalteromonas sp. NJ276

Paper ID Volume ID Publish Year Pages File Format Full-Text
4656 236 2008 7 PDF Available
Title
Purification and properties of an extracellular cold-active protease from the psychrophilic bacterium Pseudoalteromonas sp. NJ276
Abstract

The extracellular cold-active protease from the psychrophilic bacterium Pseudoalteromonas sp. NJ276 was purified by 22.5-fold using precipitate of saturation (NH4)2SO4, DEAE-Sephadex A50 and Sephadex G-75. It was shown that purified enzyme was homogeneous in terms of SDS-PAGE with molecular mass estimate of 28 kDa. The protease depicted an optimal pH of 8.0 and was stable at pH 7.0–9.0, and its optimal temperature was at 30 °C. The protease was completely inhibited by PSFM. It was partially inhibited by metal salts, especially, had high tolerance to a wide range of NaCl concentrations (0–3 M NaCl). The highest kcat and kcat/Km values were observed at 35 °C, and 35 and 54% of their highest values retained at 0 °C, respectively. Milk protein treated by this protease released more free amino acids than those treated by mesophilic papain at 4 °C. These results suggested that Pseudoalteromonas sp. NJ276 protease had broad substrate specificities and potential application in low-temperature food processing.

Keywords
Cold-active protease; Purification; Psychrophilic bacterium; Pseudoalteromonas sp.
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Purification and properties of an extracellular cold-active protease from the psychrophilic bacterium Pseudoalteromonas sp. NJ276
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 38, Issue 3, 15 March 2008, Pages 362–368
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
Price after discount Only $4.95
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Full-text PDF Download
Online Support
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