Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies
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 n...
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crwiley:10.1002/jsfa.11749 2024-06-09T07:40:39+00:00 Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies Chen, Wenyi He, Lihong Song, Wenzhu Huang, Jianrong Zhong, Nanjing National Natural Science Foundation of China 2022 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 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of the Science of Food and Agriculture volume 102, issue 10, page 4012-4024 ISSN 0022-5142 1097-0010 journal-article 2022 crwiley https://doi.org/10.1002/jsfa.11749 2024-05-16T14:26:27Z 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 ... Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Journal of the Science of Food and Agriculture 102 10 4012 4024 |
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Wiley Online Library |
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English |
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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 ... |
author2 |
National Natural Science Foundation of China |
format |
Article in Journal/Newspaper |
author |
Chen, Wenyi He, Lihong Song, Wenzhu Huang, Jianrong Zhong, Nanjing |
spellingShingle |
Chen, Wenyi He, Lihong Song, Wenzhu Huang, Jianrong Zhong, Nanjing Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
author_facet |
Chen, Wenyi He, Lihong Song, Wenzhu Huang, Jianrong Zhong, Nanjing |
author_sort |
Chen, Wenyi |
title |
Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
title_short |
Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
title_full |
Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
title_fullStr |
Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
title_full_unstemmed |
Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
title_sort |
encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies |
publisher |
Wiley |
publishDate |
2022 |
url |
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 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of the Science of Food and Agriculture volume 102, issue 10, page 4012-4024 ISSN 0022-5142 1097-0010 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/jsfa.11749 |
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Journal of the Science of Food and Agriculture |
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102 |
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10 |
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4012 |
op_container_end_page |
4024 |
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1801384018572214272 |