Multi-Enzymatic Cascade for Efficient Deracemization of dl-Pantolactone into d-Pantolactone

• Published in: Molecules (Basel, Switzerland) Switzerland), 2023-07, Vol.28 (14), p.5308
• Main Authors: Jin, Lijun, Liu, Xun, Wang, Tairan, Wang, Yi, Zhou, Xueting, Mao, Wangwei, Zhang, Yinjun, Wang, Zhao, Sun, Jie, Ying, Xiangxian
• Format: Article
• Language: English
• Subjects: Biocatalysts; conjugated polyketone reductase; Dehydrogenases; deracemization; dl -pantolactone; E coli; Efficiency; Enzymes; Glucose; Instrument industry; l -pantolactone dehydrogenase; multi-enzymatic cascade; Plasmids; Solvents
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules28145308

d-pantolactone is an intermediate in the synthesis of d-pantothenic acid, which is known as vitamin B . The commercial synthesis of d-pantolactone is carried out through the selective resolution of dl-pantolactone catalyzed by lactone hydrolase. In contrast to a kinetic resolution approach, the deracemization of dl-pantolactone is a simpler, greener, and more sustainable way to obtain d-pantolactone with high optical purity. Herein, an efficient three-enzyme cascade was developed for the deracemization of dl-pantolactone, using l-pantolactone dehydrogenase from ( LPLDH), conjugated polyketone reductase from ( CPR), and glucose dehydrogenase from ( GDH). The LPLDH was used to catalyze the dehydrogenated l-pantolactone into ketopantolactone; the CPR was used to further catalyze the ketopantolactone into d-pantolactone; and glucose dehydrogenase together with glucose fulfilled the function of coenzyme regeneration. All three enzymes were co-expressed in strain BL21(DE3), which served as the whole-cell biocatalyst. Under optimized conditions, 36 h deracemization of 1.25 M dl-pantolactone d-pantolactone led to an value of 98.6%, corresponding to productivity of 107.7 g/(l·d).