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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제30권 제9호
- 발행연도
- 2020.1
- 수록면
- 1,436 - 1,442 (7page)
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초록· 키워드
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Amylosucrase (ASase, E.C. 2.4.1.4) is capable of efficient glucose transfer from sucrose, acting as the sole donor molecule, to various functional acceptor compounds, such as polyphenols and flavonoids. An ASase variant from Deinococcus geothermalis, in which the 226th alanine is replaced with asparagine (DgAS-A226N), shows increased polymerization activity due to changes in the flexibility of the loop near the active site. In this study, we further investigated how the mutation modulates the enzymatic activity of DgAS using molecular dynamics and docking simulations to evaluate interactions between the enzyme and phenolic compounds. The computational analysis revealed that the A226N mutation could induce and stabilize structural changes near the substratebinding site to increase glucose transfer efficiency to phenolic compounds. Kinetic parameters of DgAS-A226N and WT DgAS were determined with sucrose and 4-methylumbelliferone (MU) as donor and acceptor molecules, respectively. The kcat/Km value of DgAS-A226N with MU (6.352 mM-1min-1) was significantly higher than that of DgAS (5.296 mM-1min-1). The enzymatic activity was tested with a small phenolic compound, hydroquinone, and there was a 1.4-fold increase in α-arbutin production. From the results of the study, it was concluded that DgAS-A226N has improved acceptor specificity toward small phenolic compounds by way of stabilizing the active conformation of these compounds.
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참고문헌 (26)
참고문헌 신청
Moon YH / 2006 / Enzymatic synthesis and characterization of novel epigallocatechin gallate glucosides / J. Mol. Catalysis B : Enzymatic 40:1~7
Li D / 2004 / Biotechnological production of highly soluble daidzein glycosides using Thermotoga maritima maltosyltransferase / J. Agric. Food Chem 52:2561~2567
Bae HK / 2002 / Modification of ascorbic acid using transglycosylation activity of Bacillus stearothermophilus maltogenic amylase to enhance its oxidative stability / J. Agric. Food Chem 50:3309~3316
Liang C / 2016 / Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification / Sci. Rep 6:21051
서동호 / 2020 / Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase / Food Science and Biotechnology 29(1):1~16
Li D / 2004 / Biotechnological production of highly soluble daidzein glycosides using Thermotoga maritima maltosyltransferase / J. Agric. Food Chem 52:2561~2567
Bae HK / 2002 / Modification of ascorbic acid using transglycosylation activity of Bacillus stearothermophilus maltogenic amylase to enhance its oxidative stability / J. Agric. Food Chem 50:3309~3316
Liang C / 2016 / Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification / Sci. Rep 6:21051
서동호 / 2020 / Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase / Food Science and Biotechnology 29(1):1~16
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