Abstract
The specificity and mode of action ofAspergillus sojae carboxyl proteinase I were investigated with the oxidized B-chain of insulin.A. sojae carboxyl proteinase I hydrolyzed primarily two peptide bonds in the oxidized B-chain of insulin, the Leu15-Tyr16 bond and the Phe24-Phe25 bond. Additional cleavage of the bond Tyr16-Leu17 was also noted.
Similar content being viewed by others
Literature Cited
Craig, L. C., Konigsberg, W., King, T. P. 1961. Peptide chains (A and B) from beef insulin. Biochemical Preparations8:70–75.
Frankel-Conrat, H., Harris, J. I., Levy, A. L. 1955. Recent developments in techniques for terminal and sequence studies in peptides and proteins, pp. 359–425. In: Glick, D. (ed.), Methods in biochemical analysis, vol. II. New York: Interscience.
Gabriel, O. 1971. Analytical disc gel electrophoresis, pp. 565–578. In: Jakoby, W. B. (ed.) Methods in enzymology, vol. XXII. New York: Academic Press.
Griffin, T. B., Wagner, F. W., Prescott, J. M. 1966. Anion exchange chromatography of oxidized insulin peptides. Journal of Chromatography23:280–286.
Hayashi, K., Mizunuma, T. 1974. Acid proteinase from soy sauce brewing fungusAspergillus sojae, p. 42. In: Abstract Papers of Agricultural Chemical Society of Japan. Tokyo: Agricultural Chemical Society of Japan.
Ichihara, S., Uchino, F. 1975. The specificity of acid proteinase fromAcrocylindrium. Agricultural Biological Chemistry39:423–428.
Ichishima, E. 1970. Purification and mode of assay for acid proteinase ofAspergillus saitoi, pp. 397–406. In: Perlmann, G. E., Lorand, L. (eds.), Methods in enzymology New York: Academic Press.
Ichishima, E. 1972. Purification and characterization of a new type of acid carboxypeptidase fromAspergillus saitoi. Biochimica et Biophysica Acta293:444–450.
IUPAC and IUB Recommendations. 1972. Units of enzyme activity, pp. 26–27. In: Comprehensive biochemistry. Enzyme nomenclature, vol. 13. Amsterdam: Elsevier
Mains, G., Takahashi, M., Sodek, J., Hofmann, T. 1971. The specificity of penicillopepsin. Canadian Journal of Biochemistry49:1134–1149.
Oda, K., Murao, S. 1976. Action ofScytalidium lignicolumn acid proteinases on insulin B-chain. Agricultural Biological Chemistry40:1221–1225.
Reichelt, D., Jacobson, E., Haschen, R. T. 1974. Purification and properties of cathepsin D from human erythrocytes. Biochimica et Biophysica Acta341:15–26.
Roberts, N. B., Taylor, W. H. 1978. The isolation and properties of a non-pepsin proteinase from human gastric mucosa. Biochemical Journal169:617–624.
Roberts, N. B., Taylor, W. H. 1979. Action of human pepsins 1, 2, 3 and 5 on the oxidized B-chain of insulin. Biochemical Journal179:183–190.
Ryle, A. P., Lecherc, J., Falla, F. 1968. The substrate specificity of pepsin C. Biochemical Journal110:4p.
Sanger, F., Tuppy, H. 1951. The amino acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochemical Journal49:481–490.
Tanaka, N., Takeuchi, M., Ichishima, E. 1977. Purification of an acid proteinase fromAspergillus saitoi and determination of peptide bond specificity. Biochimica et Biophysica Acta485:406–416.
Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T., Fukumoto, J. 1969. Studies on mold proteases. Part II. Substrate specificity of acid protease ofRhizopus chinensis. Agricultural Biological Chemistry33:1419–1426.
Vesterberg, O. 1971. Isoelectric focusing of proteins, pp. 389–412. In: Jakoby, W. B. (ed.), Methods in enzymology, vol. XXII. New York: Academic Press.
Yamamoto, K., Hayashi, K. 1961. Proteinase-inhibitor from the cell free extract ofAspergillus sojae and its inactivation. Symposium of Enzyme Chemistry, Japan13:137–139.
Yong, F. M., Wood, B. J. B. 1974. Microbiology and biochemistry of soy sauce fermentation, pp. 157–194. In: Perlman, D. (ed.), Advances in applied microbiology, vol. 17. New York: Academic Press.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kimura, T., Mayumi, Y., Takeuchi, M. et al. Substrate specificity of carboxyl proteinase ofAspergillus sojae . Current Microbiology 3, 153–156 (1979). https://doi.org/10.1007/BF02601858
Issue Date:
DOI: https://doi.org/10.1007/BF02601858