Encapsulation of lipases on coordination polymers and their catalytic performance in glycerolysis and esterification

In this study, lipases of CALB (Candida antarctica lipase B), TLL (Thermomyces lanuginosa lipase), RML (Rhizomucor miehei lipase), CALA (Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into the nucleotide-hybrid metal coordination polymers (CPs) for diacylglyerols (DAG) prepa...

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Bibliographic Details
Published in:Grain & Oil Science and Technology
Main Authors: Can Zeng, Nanjing Zhong
Format: Article in Journal/Newspaper
Language:English
Published: KeAi Communications Co., Ltd. 2023
Subjects:
Lipase
Coordination polymers
Encapsulation
Glycerolysis
Esterification
Agriculture
S
Food processing and manufacture
TP368-456
Antarc*
Antarctica
Online Access:https://doi.org/10.1016/j.gaost.2023.04.001
https://doaj.org/article/1fdaccfe4e144533b56d00ee0e24200d
Description
Summary:In this study, lipases of CALB (Candida antarctica lipase B), TLL (Thermomyces lanuginosa lipase), RML (Rhizomucor miehei lipase), CALA (Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into the nucleotide-hybrid metal coordination polymers (CPs) for diacylglyerols (DAG) preparation. Guanosine 5′-monophosphate (GMP) and adenosine 5′-monophosphate (AMP) were used as coordinating molecules, and metal ions of Fe3+, Ba2+, Mn2+, Ni2+ and Cr3+ were applied to prepare matrix. Results indicated that, besides Ba2+ with AMP, all other metal ions can coordinate with AMP and GMP to generate CPs. In addition, the AMP/Ni was amorphous when standing temperature was 4 °C, while it was crystalline when standing temperature was from 30 to 180 °C. DAG content from 47.55% to 64.99% was obtained from glycerolysis by CALB@GMP/Ba, RML@GMP/Ba, TLL@GMP/Ba, RML@GMP/Mn and TLL@GMP/Mn. Additionally, CALB@GMP/Fe showed selectivity towards DAG formation in the esterification and DAG content up to 61.88% was obtained.

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