Heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum for luteolin glucoside production

被引:7
作者
Chin, Young-Wook [1 ]
Jang, Se-Won [2 ,3 ]
Shin, Hee-Soon [4 ]
Kim, Tae-Wan [1 ]
Kim, Sun-Ki [5 ]
Park, Cheon-Seok [6 ,7 ]
Seo, Dong-Ho [8 ]
机构
[1] Korea Food Res Inst, Res Grp Tradit Food, Wonju 55365, South Korea
[2] Korea Food Res Inst, Res Grp Healthcare, Wonju 55365, South Korea
[3] Gachon Univ, Dept Food Sci & Biotechnol, Coll BioNano Technol, Seongnam 13120, South Korea
[4] Korea Food Res Inst, Res Grp Nat Mat & Metab, Wonju 55365, South Korea
[5] Chung Ang Univ, Dept Food Sci & Technol, Anseong 17546, Gyeonggi, South Korea
[6] Kyung Hee Univ, Grad Sch Biotechnol, Yongin 17104, South Korea
[7] Kyung Hee Univ, Inst Life Sci & Resources, Yongin 17104, South Korea
[8] Jeonbuk Natl Univ, Dept Food Sci & Technol, Coll Agr & Life Sci, Jeonju 54896, South Korea
基金
新加坡国家研究基金会;
关键词
Luteolin; Transglucosylation; Amylosucrases; Deinococcus geothermalis; Corynebacterium glutamictun; Heterologous expression; PROTEIN; LOOP; BIOTRANSFORMATION; BIOSYNTHESIS; CHAPERONES; ARBUTIN; AGENT; GENE;
D O I
10.1016/j.enzmictec.2019.109505
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Amylosucrase (ASase) has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization. In the present study, the properties of Deinococcus geothermalis ASase (DGAS) expressed in Corynebacterium glutamicum (cDGAS) and purified via Ni-NTA affinity chromatography were compared to those of DGAS expressed in Escherichia coli (eDGAS). The pH profile of cDGAS was similar to that of eDGAS, whereas the temperature profile of cDGAS was lower than that of eDGAS. The melting temperature of both enzymes did not differ significantly. Interestingly, polymerization activity was slightly lower in cDGAS than in eDGAS, whereas luteolin (an acceptor molecule) transglucosylation activity in cDGAS was 10 % higher than that in eDGAS. Analysis of protein secondary structure via circular dichroism spectroscopy revealed that cDGAS had a lower strand/helix ratio than eDGAS. The present results indicate that cDGAS is of greater industrial significance than eDGAS.
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页数:8
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