Enzymatic Production of High Concentration Glucose-1-Phosphate

JOURNAL OF CHEMICAL ENGINEERING OF JAPAN

Masaru Sakata²  Takashi Kawai¹  Hiroshi Ooshima²  Shigeto Kayane³ 

[1] Processing Development Research Laboratories, Kao Corp.;Department of Applied and Bioapplied Chemistry, Graduate School of Engineering, Osaka City University;Research & Development Division, Kao Corp.

关键词: Phosphorylase;    Glucose-1-Phosphate;    G-1-P;    Glucan;    Phosphate;    High Concentration;   

DOI  :  10.1252/jcej.07we298

来源: Maruzen Company Ltd

【 摘 要 】

References(14)Cited-By(1)Glucose-1-phosphate (G-1-P) is a biological product which, along with its derivatives, has various physiological applications. In order to develop an efficient industrial process for G-1-P, enzymatic production of high concentration G-1-P was attempted by using phosphorylase purified from potatoes as an enzyme, several kinds of linear and branched dextrin differing in chain length and a mixture of KH2PO4 and K2HPO4 (Pi) as substrates. Since the maltotetraose is not active as a substrate for production of G-1-P, effective glucan concentration was defined on a basis of moles of glucose (CeG) excluding a segment of maltotetraose from dextrin. Furthermore, since the reaction was a complicated reversible reaction involving many kinds of glucan differing in chain length, the inhibitory effect of a high concentration of substrate for the enzyme, an apparent equilibrium constant Kapp was defined. Kapp was expressed as a function of initial concentration of glucan (CeG,0) and phosphate (CP,0). The concentration of G-1-P finally obtained at the equilibrium (CG1P,eq) could be easily calculated from Kapp regardless of chain length and branch structures of glucan. As a result, a diagram expressing CG1P,eq as a function of CeG,0 and CP,0 was proposed. A high concentration of G-1-P, namely 230 mM G-1-P was experimentally obtained when CeG,0 and CP,0 were 516 and 3000 mM, respectively, and the enzymatic activity was 100 U·mL–1.

【 授权许可】

Unknown