Kinetics of Thermal Inactivation of Penaeus penicillatus Acid Phosphatase

P.-Z. Yang¹, Q.-X. Chen^1,2, Z.-X. Xie¹, S.-L. Chen¹, Y. Yang², Y.-D. Park², and H.-M. Zhou^2*

¹Department of Biology, Xiamen University, Xiamen 361005, People's Republic of China

²Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China; E-mail: zhm-dbs@mail.tsinghua.edu.cn

^* To whom correspondence should be addressed.

Received July 27, 1998

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The kinetics of thermal inactivation of Penaeus penicillatus acid phosphatase have been studied using a kinetic method related to the substrate reaction during irreversible inhibition of the enzyme activity as previously described by Tsou (Adv. Enzymol. Relat. Areas Mol. Biol. (1988) 61, 381-436). The kinetics of thermal inactivation of the enzyme show that the reaction is irreversible. The microscopic rate constants were determined for thermal inactivation of free enzyme and the enzyme--substrate complex. The results show that the presence of substrate has a significant protective effect against thermal inactivation of the enzyme.

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KEY WORDS: acid phosphatase, kinetic analysis, thermal inactivation

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