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

Wang, Quanfu; Hou, Yanhua; Xu, Zhenbo; Miao, Jun; Guang-you, LI

doi:10.1016/j.bej.2007.07.025

Cited by 45 publications

(28 citation statements)

References 15 publications

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“…The optimum temperature for the protease of Pseudoalteromonas sp. NJ276 (Wang et al 2008) was 30°C, which is consistent with the present study.…”

Section: Characterization Of Purified Proteasesupporting

confidence: 93%

Purification and properties of heat-stable extracellular protease from Pseudomonads fluorescens BJ-10

Zhang

2012

J Food Sci Technol

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Pseudomonas fluorescens BJ-10, a kind of psychrotrophic bacteria, was isolated from raw milk. It produced an extracellular protease of 47 kDa by SDS-PAGE. The crude proteases were purified by ammonium sulfate fractionation, ion-exchange and gel filtration chromatography. The specific activity of purified protease increased 61.38-fold. The optimum pH and temperature were pH 7.0 and 30°C, respectively. The purified protease was partially inhibited by DL-dithiothreitol, and the activity increased a little upon Fe 2+ addition. The protease showed typical heatstable behavior. After treatment at 100°C for 3 min, more than 94% activity remained. This work might lay the foundation for possible relationship between the heat stable protease and gelation of UHT milk.

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“…The optimum temperature for the protease of Pseudoalteromonas sp. NJ276 (Wang et al 2008) was 30°C, which is consistent with the present study.…”

Section: Characterization Of Purified Proteasesupporting

confidence: 93%

Purification and properties of heat-stable extracellular protease from Pseudomonads fluorescens BJ-10

Zhang

2012

J Food Sci Technol

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“…The purification of protease was performed according to the methods of Wang et al . () and Chakrabarti et al . () with some modifications.…”

Section: Methodsmentioning

confidence: 99%

Characterisation of acid proteases from a fusant F76 and its progenitors Aspergillus oryzae HN3042 and Aspergillus niger CICC2377

Wang

et al. 2013

Int J of Food Sci Tech

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Summary The characteristics of a novel acid protease from a fusant F76 were comparatively evaluated with those from its progenitors Aspergillus oryzae HN3042 and A. niger CICC2377. The UV spectra of these three acid proteases were similar, but fluorescence spectra were different. The acid protease from F76 contained 7.1% α‐helix, 39.4% β‐sheet, 24.7% β‐turn and 32% aperiodic coil, unlike those from its progenitors. The acid protease from F76 was active in the temperature range of 35–55 °C with the optimum temperature of 40 °C and was stable in the pH range of 2.5–6.5 with the optimum pH of 3.5, while those values from A. oryzae HN3042 and A. niger CICC2377 were 45 °C, 4.0 and 40 °C, 3.5, respectively. The kinetic parameters of the acid protease from F76 were different from its progenitors and the Michaelis constant, maximum velocity, activation energy, and attenuation index were 0.96 mg mL−1, 135.14 μmol min−1 mg−1, 64.11 kJ mol−1 and 0.59, respectively.

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“…Many cold‐active proteases have previously been isolated from cold‐adapted bacteria living at near‐neutral pH (Joshi and Satyanarayana, ). This includes a few subtilisin‐type proteases with temperature optima similar to those reported here, but most of these subtilisins display pH optima lower than the characterized Arsukibacterium subtilisins (Wang et al ., , ; Zhu et al ., ; Yang et al ., ). High‐alkaline subtilisins have been isolated from alkaliphilic bacteria, primarily species of Bacillus , and although special exceptions do exist, they generally have temperature optima above 60°C (Okuda et al ., ; Kobayashi et al ., ).…”

Section: Resultsmentioning

confidence: 99%

Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases

Lylloff

Hansen

Jepsen

et al. 2016

Microbial Biotechnology

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SummaryProteases active at low temperature or high pH are used in many commercial applications, including the detergent, food and feed industries, and bacteria specifically adapted to these conditions are a potential source of novel proteases. Environments combining these two extremes are very rare, but offer the promise of proteases ideally suited to work at both high pH and low temperature. In this report, bacteria from two cold and alkaline environments, the ikaite columns in Greenland and alkaline ponds in the McMurdo Dry Valley region, Antarctica, were screened for extracellular protease activity. Two isolates, Arsukibacterium ikkense from Greenland and a related strain, Arsukibacterium sp. MJ3, from Antarctica, were further characterized with respect to protease production. Genome sequencing identified a range of potential extracellular proteases including a number of putative secreted subtilisins. An extensive liquid chromatography–tandem mass spectrometry analysis of proteins secreted by A. ikkense identified six subtilisin‐like proteases as abundant components of the exoproteome in addition to other peptidases potentially involved in complete degradation of extracellular protein. Screening of Arsukibacterium genome libraries in Escherichia coli identified two orthologous secreted subtilisins active at pH 10 and 20°C, which were also present in the A. ikkense exoproteome. Recombinant production of both proteases confirmed the observed activity.

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

Cited by 45 publications

References 15 publications

Purification and properties of heat-stable extracellular protease from Pseudomonads fluorescens BJ-10

Purification and properties of heat-stable extracellular protease from Pseudomonads fluorescens BJ-10

Characterisation of acid proteases from a fusant F76 and its progenitors Aspergillus oryzae HN3042 and Aspergillus niger CICC2377

Genomic and exoproteomic analyses of cold‐ and alkaline‐adapted bacteria reveal an abundance of secreted subtilisin‐like proteases

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