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The nonaqueous catalysis of lipases is significant for synthesis of high pure esters, but they usually behave low catalytic activity due to denaturation and aggregation of enzyme protein in organic phases. To improve the nonaqueous catalysis, the inexpensive copper phthalocyanine was taken as a new carrier on which Pseudomonas cepacia lipase was immobilized by physical absorption, and used for synthesis of hexyl acetate, an important flavor, via transesterification of hexanol and vinyl acetate. Results showed that the desired loading was 10-mg lipase immobilized on 10-mg copper phthalocyanine powder. When the immobilized lipase was employed in the reaction system consisted of 1.5-mL hexanol and 1.5-mL vinyl acetate at 37°C and 160 rpm, the conversion was fivefolds of that catalyzed by native lipase after 1 h, and reached 99.0% after 8 h. In six times of 8-h reuses, the immobilized lipase behaved an activity attenuation rate 1.22% h−1, lower than 1.77% h−1 of native lipase, which meant that the immobilized lipase was more stable. Even at the room temperature and the static state without shaking or stirring, the immobilized lipase still brought conversion 42.8% after 10 h and the native lipase gave 20.1%. Obviously, the immobilized lipase is an available biocatalyst in organic phase and has great potential in food industry. [ABSTRACT FROM AUTHOR]

The nonaqueous catalysis of lipases is significant for synthesis of high pure esters, but they usually behave low catalytic activity due to denaturation and aggregation of enzyme protein in organic phases. To improve the nonaqueous catalysis, the inexpensive copper phthalocyanine was taken as a new carrier on which Pseudomonas cepacia lipase was immobilized by physical absorption, and used for synthesis of hexyl acetate, an important flavor, via transesterification of hexanol and vinyl acetate. Results showed that the desired loading was 10 mg lipase immobilized on 10 mg copper phthalocyanine powder. When the immobilized lipase was employed in the reaction system consisted of 1.5 mL hexanol and 1.5 mL vinyl acetate at 37℃ and 160 rpm, the conversion was five fold of that catalyzed by native lipase after 1 h, and reached 99.0% after 8 h. Undergoing six times of 8-h reuses, the immobilized lipase had an activity attenuation rate 1.22% h− 1, lower than 1.77% h− 1 of native lipase, which meant that the immobilized lipase was more stable. Even at the room temperature and the static state without shaking or stirring, the immobilized lipase could bring conversion 42.8% after 10 h and the native lipase gave 20.1%. Obviously, the immobilized lipase is an available biocatalyst in organic phase and has great potential in food industry. [ABSTRACT FROM AUTHOR]

This document is a retraction note for an article titled "Copper Phthalocyanine Improving Nonaqueous Catalysis of Pseudomonas cepacia Lipase for Ester Synthesis." The publisher has retracted the article because an incorrect version was published in error. The correct manuscript has been republished. The authors agree to this retraction. The document provides links to the correct version of the article. [Extracted from the article]