title: Molecular cloning and sequence analysis of an extracellular protease from four Bacillus subtilis strains.
abstract: Four Bacillus subtilis strains were isolated from traditional fermented foods, and the sequences of their extracellular alkaline proteases (AprE) were analyzed and cloned. The recombinant enzymes synthesized by means of Escherichia coli exhibited high proteolytic activity. AprE CN2 showed hydrolytic activity 4-fold higher than that of AprE 168. This activity was also seen in the presence of relatively high NaCl concentrations.
authors.affiliation: United Graduate School of Agricultural Science, Gifu University, Gifu, Japan.
authors.forename: Xujun
authors.initials: X
authors.lastname: Han
authors.forename: Yuh
authors.initials: Y
authors.lastname: Shiwa
authors.forename: Masanori
authors.initials: M
authors.lastname: Itoh
authors.forename: Tohru
authors.initials: T
authors.lastname: Suzuki
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Yoshikawa
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Nakagawa
authors.forename: Hiroko
authors.initials: H
authors.lastname: Nagano
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000166:cytology / Q000201:enzymology* / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D005110:Extracellular Space / Q000201:enzymology*; D007700:Kinetics; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D012965:Sodium Chloride / Q000494:pharmacology
chemical_list: D001426:Bacterial Proteins; D012965:Sodium Chloride; D010450:Endopeptidases; C087822:alkaline protease