Thermostable neutral protease resembling thermolysin derived from Bacillus brevis MIB001
Autor: | Yoshimi Urata, Yukio Takii, Noriko Ueno |
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Rok vydání: | 1998 |
Předmět: |
medicine.medical_treatment
Molecular Sequence Data Thermolysin Bacillus Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Microbiology Endopeptidases medicine Amino Acid Sequence Molecular Biology Soil Microbiology Thermostability chemistry.chemical_classification Metalloproteinase Protease biology fungi Organic Chemistry Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme Brevibacillus brevis chemistry bacteria Bacteria Biotechnology |
Zdroj: | Bioscience, biotechnology, and biochemistry. 62(5) |
ISSN: | 0916-8451 |
Popis: | A microbe producing a protease with strong thermostability that was released extracellularly was isolated from soil. The isolate, MIB001, grew at from 15 to 51 degrees C and pH 5.1-8.8 and was tentatively identified as a strain of Bacillus brevis. Rabbit antisera raised against a pure preparation of the protease did not cross-react with thermolysin or neutral metalloprotease from Bacillus stearothermophilus KP1236. |
Databáze: | OpenAIRE |
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