Purication and Heat-stable Properties of a Novel Protease from Pseudomonads fluorescens Rm12

Chem. J. Chinese Universities

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Purication and Heat-stable Properties of a Novel Protease from Pseudomonads fluorescens Rm12

MU Zhi-Shen^1,2, Bai Ying², ZHAO Guang-Hua¹, HU Xiao-Song¹*

1. College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China;
2. College of Food Science & Engineering, Inner Mongolia Agricultural University, Hohot 010018, China

Received:2007-07-10 Revised:1900-01-01 Online:2008-04-10 Published:2008-04-10
Contact: HU Xiao-Song

Abstract

Abstract: Heat-resistant proteases from psychrotrophic bacteria in raw milk may induce bitterness, gelation and hydrolyzation of sterilized milk. A novel extracellular heat-stable metalloprotease, named as Ht12, was found for the first time from Pseudomonads fluorescens Rm12,which was isolated from raw milk. Ht12 was purified to homogeneity from the culture supernatant via ammonium sulfate precipitation, ion-exchange chromatography, hydrophobic chromatography, and size exclusion chromatography and its properties of enzymology and heat-stable properties was studied. This protease in its native state was identified as a monomer of 45000 Da, containing Pro and disulfide bonds and the N-terminal sequence was MSKVKDKAIVSAAQAS. Mn²⁺ has positive effect on activity. The protease has a higher heat resistance. After treatment of 160 ℃ for 20 s, the residual activity was 3.8%.

Key words: Pseudomonads fluorescens, Heat-stable protease, Metalloprotease, Raw milk

CLC Number:

O629
Q55

TrendMD:

MU Zhi-Shen^1,2, Bai Ying², ZHAO Guang-Hua¹, HU Xiao-Song¹*. Purication and Heat-stable Properties of a Novel Protease from Pseudomonads fluorescens Rm12[J]. Chem. J. Chinese Universities, doi: .

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Purication and Heat-stable Properties of a Novel Protease from Pseudomonads fluorescens Rm12

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