Trypsin: A Novel Scavenger of Superoxide Anion | Abstract

e-ISSN:2320-1215 p-ISSN: 2322-0112

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Trypsin: A Novel Scavenger of Superoxide Anion

Abstract

Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. The superoxide scavenging activity of trypsin was accidentally found. Results showed that trypsin could scavenge superoxide in both intracorporal and extracorporal systems. The value of km of superoxide scavenging presented by the trypsin was 0.0618 mm The rate of superoxide scavenging increased up to 0.103 μM/μg trypsin/min with the increasing of hydrogen peroxide production rate to a maximum of 0.00122 μM/μg trypsin/min. Trypsin has an optimal operating pH of within 7.5-8.5. The scavenging activity of trypsin was accelerated by copper and impeded by chelators of metals. These indubitable results suggested that trypsin is a novel scavenger of superoxide. The rate of superoxide scavenging and hydrogen peroxide production were impacted by the concentration of trypsin or riboflavin, pH or ions. Trypsin might be a potential drug for anti-oxidant stress in human

Xin Li, Xinyue Pang, Zichen Tang, Jinle Xiang, Yunhong Liu and Jiaju Qiao

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