Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys⁴⁸

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• 作者：Jong Min Lee^a ; Soo Young Moon^a ; Yu-Ri Kim^b ; Kang Woong Kim^c ; Bong-Joo Lee^c ; In-Soo Kong^a ; ^{iskong@pknu.ac.kr}
• 关键词：β-1 ; 3-1 ; 4-Glucanase ; Thermostability ; Halostability
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：94
• 期：part_PA
• 页码：594-602
• 全文大小：2113 K
• 卷排序：94

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.