Practical resolution system for DL-pantoyl lactone using the lactonase from Fusarium oxysporum.
We developed an enzymatic resolution system for DL-pantoyl lactone that uses immobilized mycelia of Fusarium oxysporum, which produce a lactone-hydrolyzing enzyme (lactonase). The lactonase catalyzes the stereospecific hydrolysis of D-pantoyl lactone. One hundred eighty repeated batch reactions (total reaction time, 3780 h) were made with mycelia entrapped in calcium alginate gels as the catalyst, in the presence of 90 mM CaCl2. With a 300 gl(-1)DL-pantoyl lactone solution as the substrate, the hydrolysis rate for DL-pantoyl lactone was > 40% and the optical purity of D-pantoic acid was 90% enantiomer excess. Immobilized mycelia retained 70% of their initial lactonase activity, even after 180 batch reactions. The estimated half-life of the lactonase activity of the immobilized mycelia was 6000 h, which is 35 times higher than that of the free mycelia. The process has been exploited commercially since 1999.
Sakamoto
Keiji
K
Technical Department, Daiichi Fine Chemical Co., Ltd., 530 Chokeiji, Toyama 933-8511, Japan.
Honda
Kohsuke
K
Wada
Koichi
K
Kita
Shinji
S
Tsuzaki
Kazuya
K
Nose
Hanae
H
Kataoka
Michihiko
M
Shimizu
Sakayu
S
D015107:4-Butyrolactone / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D005670:Fusarium / Q000201:enzymology*; D025282:Mycelium / Q000737:chemistry / Q000378:metabolism*; D010865:Pilot Projects
D004800:Enzymes, Immobilized; C005412:pantolactone; D002265:Carboxylic Ester Hydrolases; C416845:pantoyl lactone hydrolase; D015107:4-Butyrolactone