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• W3109396009 abstract "Abstract BACKGROUND Psychrophiles have evolved to adapt to freezing environments, and cold‐adapted enzymes from these organisms can maintain high catalytic activity at low temperature. The use of cold‐adapted enzymes has great potential for the revolution of food and molecular biology industries. RESULTS In this study, four different strains producing protease were isolated from traditional fermented shrimp paste, one of which, named Planococcus maritimus XJ11 by 16S rRNA nucleotide sequence analysis, exhibited the largest protein hydrolysis clear zone surrounding the colonies. Meanwhile, the strain P. maritimus XJ11 was selected for further investigation because of its great adaptation to low temperature, low salinity and alkaline environment. The enzyme activity assay of P. maritimus XJ11 indicated that the optimum conditions for catalytic activity were pH 10.0 and 40 °C. Moreover, the enzyme also showed an increasing activity with temperatures from 10 to 40 °C and retained more than 67% activity of the maximum over a broad range of salinity (50–150 g L −1 ). Genome sequencing analysis revealed that strain XJ11 possessed one circular chromosome of 3 282 604 bp and one circular plasmid of 67 339 bp, with a total number of 3293 open reading frames (ORFs). Besides, 21 genes encoding protease, including three serine proteases, were identified through the NR database. CONCLUSION Cold‐adapted bacterium P. maritimus XJ11 was capable of producing alkaline proteases with high catalytic efficiency at low or moderate temperatures. Furthermore, the favorable psychrophilic and enzymatic characters of strain P. maritimus XJ11 seem to have a promising potential for industrial application. © 2020 Society of Chemical Industry" @default.
• W3109396009 created "2020-12-07" @default.
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• W3109396009 date "2020-12-05" @default.
• W3109396009 modified "2023-09-26" @default.
• W3109396009 title "Genome sequencing of cold‐adapted <i>Planococcus</i> bacterium isolated from traditional shrimp paste and protease identification" @default.
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• W3109396009 doi "https://doi.org/10.1002/jsfa.10952" @default.
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