title: Purification of collagenase and specificity of its related enzyme from Bacillus subtilis FS-2.
abstract: A collagenase in the culture supernatant of B. subtilis FS-2, isolated from traditional fish sauce, was purified. The enzyme had a molecular mass of about 125 kDa. It degraded gelatin with maximum activity at pH 9 and a temperature of 50 degrees C. The purified enzyme was stable over a wide range of pH (5-10) and lost only 15% and 35% activity after incubation at 60 degrees C and 65 degrees C for 30 min, respectively. Slightly inhibited by EDTA, soybean tripsin inhibitor, iodoacetamide, and iodoacetic acid, the enzyme was severely inhibited by 2-beta-mercaptoethanol and DFP. The protease from B. subtilis FS-2 culture digested acid casein into fragments with hydrophilic and hydrophobic amino acids as C-terminals, in particular Asn, Gly, Val, and Ile.
authors.affiliation: Faculty of Education, Gifu University, Japan. nagano@cc.gifu-u.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Nagano
authors.forename: K A
authors.initials: KA
authors.lastname: To
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D017364:Collagenases / Q000302:isolation & purification*; D004492:Edetic Acid / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005396:Fish Products / Q000382:microbiology; D007460:Iodoacetamide / Q000494:pharmacology; D019807:Iodoacetic Acid / Q000494:pharmacology; D007531:Isoflurophate / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D007531:Isoflurophate; D008623:Mercaptoethanol; D004492:Edetic Acid; D017364:Collagenases; D019807:Iodoacetic Acid; D007460:Iodoacetamide