Kinetic study of alkaline protease 894 for the hydrolysis of the pearl oyster Pinctada martensii

• Published in: Chinese journal of oceanology and limnology Vol. 31; no. 3; pp. 591 - 597
• Main Author: 陈忻 陈华 蔡冰娜 刘清钦 孙恢礼
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer-Verlag 01.05.2013; SP Science Press; Springer Nature B.V
• Subjects: Alkaline protease; Biology; Catalytic activity; Earth and Environmental Science; Earth Sciences; enzymatic hydrolysis; Enzymes; Enzymolysis; Flavobacterium; Flavobacterium yellowsea; Food industry; Hydrolysis; Inactivation; Kinetics; Low temperature; Marine; Marine biology; Marine molluscs; Mollusks; Oceanography; Oysters; Pearl oysters; Pinctada; Pinctada martensii; Protease; proteinases; Raw materials; Shellfish; Substrates; temperature; 动力学性质; 动力学模型; 平均相对误差; 底物浓度; 珍珠贝; 碱性蛋白酶; 酶水解; 马氏珠母贝; alkaline protease 894; kinetics model; inactivation constant; proteolysis rate; degree of hydrolysis
• ISSN: 0254-4059; 2096-5508; 1993-5005; 2523-3521
• DOI: 10.1007/s00343-013-2227-7

A new enzyme （alkaline protease 894） obtained from the marine extremophile Flavobacterium yellowsea （YS-80-122） has exhibited strong substrate-binding and catalytic activity, even at low temperature, but the characteristics of the hydrolysis with this enzyme are still unclear. The pearl oyster Pinctada martensii was used in this study as the raw material to illustrate the kinetic properties ofprotease 894. After investigating the intrinsic relationship between the degree of hydrolysis and several factors, including initial reaction pH, temperature, substrate concentration, enzyme concentration, and hydrolysis time, the kinetics model was established. This study showed that the optimal conditions for the enzymatic hydrolysis were an initial reaction pH of 5.0, temperature of 30~C, substrate concentration of 10% （w/v）, enzyme concentration of 2 500 U/g, and hydrolysis time of 160 min. The kinetic characteristics of the protease for the hydrolysis ofP. martensii were obtained. The inactivation constant was found to be 15.16/min, and the average relative error between the derived kinetics model and the actual measurement was only 3.04%, which indicated a high degree of fitness. Therefore, this study provides a basis for the investigation of the concrete kinetic characteristics of the new protease, which has potential applications in the food industry.