Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

Autor: Vinoth Kumar Ponnusamy, Jiang-Shiou Hwang, Hans-Uwe Dahms, Bin Huang, Revathi Gurunathan
Rok vydání: 2021
Předmět:
Models
Molecular
0106 biological sciences
0301 basic medicine
Aquatic Organisms
Hot Temperature
Protein Conformation
Bioconversion
medicine.medical_treatment
Bacillus cereus
Gene Expression
Biochemistry
01 natural sciences
Substrate Specificity
Serine
chemistry.chemical_compound
Enzyme Stability
Subtilisins
Cloning
Molecular
chemistry.chemical_classification
Multidisciplinary
biology
Hydrogen-Ion Concentration
Chemical biology
Recombinant Proteins
Amino acid
Keratins
Medicine
Biotechnology
Brachyura
Science
Genetic Vectors
Article
03 medical and health sciences
Hydrothermal Vents
Bacterial Proteins
010608 biotechnology
Escherichia coli
medicine
Animals
Pacific Ocean
Protease
fungi
Subtilisin
Feathers
biology.organism_classification
030104 developmental biology
Enzyme
chemistry
Proteolysis
Serine Proteases
PMSF
Chickens
Zdroj: Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Scientific Reports
ISSN: 2045-2322
DOI: 10.1038/s41598-021-90375-4
Popis: Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs.
Databáze: OpenAIRE
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