Enzymatic synthesis of astaxanthin n-octanoic acid esters.
We examined the enzymatic synthesis of astaxanthin n-octanoic acid esters. Carriers for the immobilized enzyme and reaction conditions such as water content, reaction temperature, and time were examined using Candida cylindracea lipase (Lipase OF). Lipase OF) immobilized by a hydrophobic anion exchange resin (10% w/w content of lipase) gave the best yield in the esterification reaction of astaxanthin. Two milligrams of astaxanthin per 750 microL tri-n-octanoin (ca. 0.3%) was optimum because of the low solubility of tri-n-octanoin. The esters were obtained in a yield of 36.4% under the optimal reaction conditions.
Institute for Advanced Technology, Technological Development Center, Suntory Ltd., Yamazaki, Mishima-gun, Osaka, Japan.
Masahiro
M
Nakao
Motoo
M
Sumida
Kenji
K
Katano
Harukazu
H
Fukami
D002210:Caprylates / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004951:Esterification; D004952:Esters / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors; D014867:Water / Q000378:metabolism; D024341:Xanthophylls / Q000096:biosynthesis / Q000737:chemistry
D002210:Caprylates; D004800:Enzymes, Immobilized; D004952:Esters; D024341:Xanthophylls; D014867:Water; C005948:astaxanthine; D008049:Lipase