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Lipase-Catalyzed Regioselective Synthesis of Dextrin Esters.
Biomacromolecules ( IF 5.5 ) Pub Date : 2018-11-19 , DOI: 10.1021/acs.biomac.8b01374
Hak Yong Lee 1 , Satoshi Kimura 1, 2 , Tadahisa Iwata 1
Affiliation  

Four lipase enzymes were investigated as catalysts in the synthesis of regioselectively monosubstituted dextrin esters from dextrin and vinyl acetate. An immobilized lipase enzyme (Lipozyme TL IM) exhibited the highest activity. This enzyme showed regioselective substitution of the dextrin at the primary hydroxyl group (C6 position) under optimal conditions (60 °C for 24 h, using a 1:3 molar ratio of glucose unit/vinyl acetate and 2.5 U/mL enzyme dosage in an organic solvent). To compare the reactivity of other vinyl esters, monosubstituted dextrin esters (degrees of substitution [DS] ≈ 1) with varying side-chain lengths (C2-C12) were synthesized. With increasing side-chain length, the initial catalytic activity of the lipase enzyme decreased, resulting in lower DS values. However, the final DS values of the monosubstituted dextrin esters with longer side chains were higher than those of the shorter-chain analogues, because of an increase in affinity between the substrate and acyl donor.

中文翻译:

脂肪酶催化糊精酯的区域选择性合成。

研究了四种脂肪酶作为催化剂从糊精和乙酸乙烯酯合成区域选择性单取代糊精酯的催化剂。固定化的脂肪酶(Lipozyme TL IM)表现出最高的活性。该酶在最佳条件下(60°C持续24小时)显示出在伯羟基(C6位置)上糊精的区域选择性取代,使用1:3的葡萄糖单位/乙酸乙烯酯摩尔比和2.5 U / mL的酶剂量。有机溶剂)。为了比较其他乙烯基酯的反应性,合成了具有不同侧链长度(C2-C12)的单取代糊精酯(取代度[DS]≈1)。随着侧链长度的增加,脂肪酶的初始催化活性降低,从而导致DS值降低。然而,
更新日期:2018-11-06
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