Autoproteolysis of Procerain and Procerain B mediated by structural changes

• Published in: Phytochemistry (Oxford) Vol. 196; p. 113086
• Main Authors: Srivastava, Gaurav, Gaur, Neeraj, Makde, Ravindra D., Jamdar, Sahayog N.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.04.2022
• Subjects: Autolysis; Calotropis; Calotropis procera; Cysteine Endopeptidases; DSF; Latex - chemistry; Procerain; Procerain B; Proteases; Structural stability; Autolysis; Procerain; Structural stability; Proteases; DSF; Procerain B; Calotropis procera
• ISSN: 0031-9422; 1873-3700
• DOI: 10.1016/j.phytochem.2022.113086

Procerain (Pc) and Procerain B (PcB) are two latex proteases from Calotropis procera having potential applications in food and other industries. However, autolytic degradation of these proteases limits their potential use in industry. Nevertheless, basic mechanism underlying the autoproteolysis has not been detailed. In order to understand the same, we subjected the enzymes to various denaturing and activating conditions. The results showed that structural changes induced by different denaturing conditions trigger their autoproteolysis. We also observed differential response of Pc, PcB and other papain-like proteases towards autocatalysis in presence of reducing agent in-spite of sharing the same structural fold, including the number of disulfide bonds. The possible reason underlying this intriguing observation is also discussed. Further, present work establishes that structural changes in the proteases lead to autoproteolysis and the enzymes are stable unless they experience structural perturbation. These findings could thus be useful for their practical applications in industries. [Display omitted] •Stable cysteine proteases from Calotropis procera latex exhibit autodegradation.•Thermal or chemical denaturation lead to rapid & extensive auto-proteolysis.•Conformational changes lead to autodegradation.•Reducing agent causes shift in the melting temperature and ensues self-digestion.