Some physicochemical properties and amino acid composition of the alkaline protease of B. amylosacchariticus were determined. The molecular weight and sedimentation coef-ficient were estimated to be 22, 700 and 2.89s, respectively, and the amino terminal amino acid was identified to be alanine. The enzyme contained 15.9% of nitrogen and was composed of 220 residues of amino acid: lys6, his5, arg3, asp20, thr14, ser37, glu12, pro10, glY25, ala27, val20, met3, isoleu12, leu12, tyr9, phe2, try3 and amide ammonia16. The results indicate that protein nature and chemical properties of the alkaline protease presented here are distinct from those of alkaline proteases obtained from the other strains of B. subtilis, such as subtilopeptidase A, B and BPN'
No takes yet. Share an insight, caveat, or question.
TSURU et al. (1967) studied this question.