Journal of Protein Chemistry 2001-02-01

Thermal stability and enzymatic activity of a smaller lysozyme from silk moth (Bombyx mori).

K Masaki, T Aizawa, N Koganesawa, T Nimori, H Bando, K Kawano, K Nitta

Index: J. Protein Chem. 20(2) , 107-13, (2001)

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Abstract

Bombyx mori lysozyme is 10 amino acids shorter than hen egg-white lysozyme, which is a typical c-type lysozyme. It was expressed by using the methylotrophic yeast Pichia pastoris. The thermal stability and the enzymatic activity of the Bombyx mori lysozyme were estimated and compared with those of human and hen egg-white lysozymes. The denaturation temperature was 17-26 degrees C lower than those of human and hen egg-white lysozymes. Further, the enthalpy change and the heat capacity change for unfolding were smaller than those of human lysozyme. It was also confirmed that the stability against guanidine hydrochloride was lower than those of the other two lysozymes. The enzymatic activity toward a simple synthetic substrate was measured and compared with those of human and hen egg-white lysozymes. The B-F binding mode was obviously dominant, although the A-E binding mode was preferred in human and hen egg-white lysozymes.