期刊
MARINE DRUGS
卷 17, 期 6, 页码 -出版社
MDPI
DOI: 10.3390/md17060378
关键词
alginate lyase; thermal stability; rational design; disulfide bond; molecular dynamic simulation
资金
- Shandong Province Key Research and Development Project [2017YYSP003]
- Natural Science Foundation of Shandong Province [ZR2017MD006]
Alginate lyase degrades alginate by the beta -elimination mechanism to produce oligosaccharides with special bioactivities. The low thermal stability of alginate lyase limits its industrial application. In this study, introducing the disulfide bonds while using the rational design methodology enhanced the thermal stability of alginate lyase cAlyM from Microbulbifer sp. Q7. Enzyme catalytic sites, secondary structure, spatial configuration, and molecular dynamic simulation were comprehensively analyzed. When compared with cAlyM, the mutants D102C-A300C and G103C-T113C showed an increase by 2.25 and 1.16 h, respectively, in half-life time at 45 degrees C, in addition to increases by 1.7 degrees C and 0.4 degrees C in the melting temperature, respectively. The enzyme-specific activity and k(cat)/K-m values of D102C-A300C were 1.8- and 1.5-times higher than those of cAlyM, respectively. The rational design strategy that was used in this study provides a valuable method for improving the thermal stability of the alginate lyase.
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