Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies

• Published in: Journal of the Science of Food and Agriculture
• Main Authors: Chen, Wenyi, He, Lihong, Song, Wenzhu, Huang, Jianrong, Zhong, Nanjing
• Other Authors: National Natural Science Foundation of China
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2022
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/jsfa.11749; https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.11749; https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsfa.11749

Abstract BACKGROUND In the present study, lipases of TLL (lipase from Thermomyces lanuginosus ), AOL (lipase from Aspergillus oryzae ), RML (lipase from Rhizomucor miehei ), BCL (lipase from Burkholderia cepacia ), CALA ( Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into nucleotide‐hybrid metal coordination polymers (CPs). Enzyme concentration was optimized for encapsulation and the enzymatic properties of the obtained lipases were investigated. In addition, their performance in glycerolysis and esterification was evaluated, and glycerolysis conditions (water content, temperature and time) were optimized. RESULTS Hydrolysis activity over 10 000 U g −1 and activity recovery over 90% were observed from AOL@GMP/Tb, TLL@GMP/Tb and RML@GMP/Tb. GMP/Tb encapsulation (of AOL, TLL, RML and LU) improved their thermostability when incubated in air. The encapsulated lipases exhibited moderate [triacylglycerols (TAG) conversion 30–50%] and considerable glycerolysis activity (TAG conversion over 60%). TAG conversions from 69.37% to 82.35% and diacylglycerols (DAG) contents from 58.62% to 64.88% were obtained from CALA@GMP/metal samples (except for CALA@GMP/Cu). Interestingly, none of the encapsulated lipases initiated the esterification reaction. AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb showed good reusability in glycerolysis, with 88.80%, 94.67%, 89.85% and 78.16% of their initial glycerolysis activity, respectively, remaining after five cycles of reuse. The relationships between temperature and TAG conversion were Ln V 0 = 6.5364–3.7943/T and Ln V 0 = 13.8820–6.4684/T for AOL@GMP/Tb and CALA@GMP/Tb, respectively; in addition, their activation energies were 31.55 and 53.78 kJ mol −1 , respectively. CONCLUSION Most of the present encapsulated lipases exhibited moderate and considerable glycerolysis activity. In addition, AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb exhibited good reusability in glycerolysis reactions and potential in practical applications. © 2022 Society of Chemical ...