Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys48
文摘
The β-1,3-1,4-glucanase was increased thermostability and halostability by substituting hydrophobic residue for Lys48. The half-lives of K48A and K48L, were significantly increased more than 3-fold in thermal and high salinity conditions. The mutant enzymes were more active and stable than their wild-type in ionic liquids.