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

Xin Chen; Hua Chen; Bingna Cai; Qingqin Liu; Huili Sun

doi:10.1007/s00343-013-2227-7

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

Updated：2023-05-16

- Kinetic study of alkaline protease 894 for the hydrolysis of the pearl oyster Pinctada martensii
- Journal of Oceanology and Limnology Vol. 31, Issue 3, Pages: 591-597(2013)
- Affiliations：
  
  1. Science School of Foshan University
  2. Key Laboratory of Marine Bio-resources Sustainable Utilization South China Sea Institute of Oceanology Chinese Academy of Sciences
  3. Graduate University of Chinese Academy of Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-013-2227-7
  CLC：
- Online First：08 May 2013，
  
  Published：2013
- Accepted：
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Chen, X., Chen, H., Cai, B. et al. Kinetic study of alkaline protease 894 for the hydrolysis of the pearl oyster Pinctada martensii, ., Chin. J. Ocean. Limnol. 31, 591–597 (2013). https://doi.org/10.1007/s00343-013-2227-7
DOI：

Chen, X., Chen, H., Cai, B. et al. Kinetic study of alkaline protease 894 for the hydrolysis of the pearl oyster Pinctada martensii, ., Chin. J. Ocean. Limnol. 31, 591–597 (2013). https://doi.org/10.1007/s00343-013-2227-7 DOI：

摘要

Abstract

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 of protease 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 of P. 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.

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Keywords

references

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