Abstract
Incubation of highly purified α-amylase fromAspergillus oryzae (EC 3.2.1.1) with 0.01M acetate buffer, pH 3.0, resulted in degradation of the α-amylase. The molecular weight values of degradation products were 42 K, 37 K, and 28 K. Incubation of the purified α-amylase in 0.02m phosphate buffer, pH 7.5, at 30°C for 17 h, however, resulted in no degradation of the α-amylase molecule.
Incubation of the purified α-amylase with proangiotensin at pH 3.0 for 24 h resulted in cleavage of Tyr4-Ile5, His6-Pro7, Pro7-Phe8, Phe8-His9, and His9-Leu10. Thus, it appears that proteolytic activities firmly bound to α-amylase are identical withAspergillus aspartic proteinase (EC 3.4.23.6) andAspergillus acid carboxypeptidase (EC 3.4.16.1).
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Hanzawa, S., Odagawa, A., Sakata, H. et al. Degradation of α-amylase fromAspergillus oryzae with firmly bound proteinases at pH 3.0. Current Microbiology 14, 235–239 (1986). https://doi.org/10.1007/BF01568525
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DOI: https://doi.org/10.1007/BF01568525