원문정보
초록
영어
Lipase B from Candida antarctica (CalB) showing several excellent characteristics such as high stereo-selectivity and stability in organic solvent has attracted much attention for various enzymatic bioconversion reactions [1]. To apply lipase to commercial process, the thermal stability is one of the prerequisites. In this study, we improved the thermal stability of CalB by increasing the number of disulfide bridges based on B-factor. MODIP program was used to determine the probability of a disulfide bridge formation between two adjacent amino acid
residues. As a result, 21 amino acid couples with the highest possibility (grade A) were firstly chosen for further investigation. Among those couples in grade A, we selected four candidates (S50-A273, Q156-L163, A162-K308, N169-F304) based on B-factor of its residues. Four double CalB mutants (S50C-A273C. Q156C-L163C, A162C-K308C and N169C-F304C) were constructed and investigated to determine the thermal stability. Two mutants A162C-K308C and N169C-F304C showed improved thermal stability compared to its wild type. We anticipate that those mutants will be one of the good candidates for further study to improve the thermal stability of CalB.