[Synthesis of glucose laurate monoester catalyzed by Candida antarctica lipase B-displaying Pichia pastoris whole-cells].
We developed a new enzymatic-catalyzing producing process of glucose laurate monoester. In the process we used Candida antarctica lipase B-displaying Pichia pastoris whole-cells as biocatalyst, glucose as the acyl acceptor and lauric acid as the acyl donor. The product glucose laurate monoester was purified by silica gel column chromatography and preparative liquid chromatography, and identified by liquid chromatography-mass spectrometry. Then we optimized the process from various aspects, such as solvent composition, ratio of dmethyl sulfoxide to 2-Methyl-2-butanol (V/V), catalyst dosage, substrate concentration, water activity and temperature. The optimal reaction conditions were: glucose 0.5 mmol/L, lauric acid 1.0 mmol/L, ratio of 2-Methyl-2-butanol to Dmethyl sulfoxide is 7:3 in 5 mL volume, temperature 60 degrees C, the best initial water activity of whole-cells biocatalyst is 0.11. The maximum glucose conversion could be 48.7% after 72 h.
Zheng
Suiping
S
Key Laboratory of Fermentation and Enzyme Engineering, School ofBioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
Ren
Changqiong
C
Han
Shuangyan
S
Lin
Ying
Y
D055162:Biocatalysis; D002175:Candida / Q000201:enzymology; D004952:Esters / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins; D005818:Genetic Engineering; D005947:Glucose / Q000737:chemistry / Q000378:metabolism*; D007848:Laurates / Q000737:chemistry / Q000378:metabolism*; D008049:Lipase / Q000096:biosynthesis* / Q000235:genetics; D010843:Pichia / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D004952:Esters; D005656:Fungal Proteins; D007848:Laurates; D011994:Recombinant Proteins; D008049:Lipase; C431349:lipase B, Candida antarctica; D005947:Glucose