Cargando…

Progress and perspectives of enzymatic preparation of human milk fat substitutes

Human milk fat substitutes (HMFS) with triacylglycerol profiles highly similar to those of human milk fat (HMF) play a crucial role in ensuring the supply in infant nutrition. The synthesis of HMFS as the source of lipids in infant formula has been drawing increasing interest in recent years, since...

Descripción completa

Detalles Bibliográficos
Autores principales: Liu, Zeqing, Dai, Lingmei, Liu, Dehua, Du, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9635142/
https://www.ncbi.nlm.nih.gov/pubmed/36333804
http://dx.doi.org/10.1186/s13068-022-02217-8
_version_ 1784824645127503872
author Liu, Zeqing
Dai, Lingmei
Liu, Dehua
Du, Wei
author_facet Liu, Zeqing
Dai, Lingmei
Liu, Dehua
Du, Wei
author_sort Liu, Zeqing
collection PubMed
description Human milk fat substitutes (HMFS) with triacylglycerol profiles highly similar to those of human milk fat (HMF) play a crucial role in ensuring the supply in infant nutrition. The synthesis of HMFS as the source of lipids in infant formula has been drawing increasing interest in recent years, since the rate of breastfeeding is getting lower. Due to the mild reaction conditions and the exceptionally high selectivity of enzymes, lipase-mediated HMFS preparation is preferred over chemical catalysis especially for the production of lipids with desired nutritional and functional properties. In this article, recent researches regarding enzymatic production of HMFS are reviewed and specific attention is paid to different enzymatic synthetic route, such as one-step strategy, two-step catalysis and multi-step processes. The key factors influencing enzymatic preparation of HMFS including the specificities of lipase, acyl migration as well as solvent and water activity are presented. This review also highlights the challenges and opportunities for further development of HMFS through enzyme-mediated acylation reactions.
format Online
Article
Text
id pubmed-9635142
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-96351422022-11-05 Progress and perspectives of enzymatic preparation of human milk fat substitutes Liu, Zeqing Dai, Lingmei Liu, Dehua Du, Wei Biotechnol Biofuels Bioprod Review Human milk fat substitutes (HMFS) with triacylglycerol profiles highly similar to those of human milk fat (HMF) play a crucial role in ensuring the supply in infant nutrition. The synthesis of HMFS as the source of lipids in infant formula has been drawing increasing interest in recent years, since the rate of breastfeeding is getting lower. Due to the mild reaction conditions and the exceptionally high selectivity of enzymes, lipase-mediated HMFS preparation is preferred over chemical catalysis especially for the production of lipids with desired nutritional and functional properties. In this article, recent researches regarding enzymatic production of HMFS are reviewed and specific attention is paid to different enzymatic synthetic route, such as one-step strategy, two-step catalysis and multi-step processes. The key factors influencing enzymatic preparation of HMFS including the specificities of lipase, acyl migration as well as solvent and water activity are presented. This review also highlights the challenges and opportunities for further development of HMFS through enzyme-mediated acylation reactions. BioMed Central 2022-11-04 /pmc/articles/PMC9635142/ /pubmed/36333804 http://dx.doi.org/10.1186/s13068-022-02217-8 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Liu, Zeqing
Dai, Lingmei
Liu, Dehua
Du, Wei
Progress and perspectives of enzymatic preparation of human milk fat substitutes
title Progress and perspectives of enzymatic preparation of human milk fat substitutes
title_full Progress and perspectives of enzymatic preparation of human milk fat substitutes
title_fullStr Progress and perspectives of enzymatic preparation of human milk fat substitutes
title_full_unstemmed Progress and perspectives of enzymatic preparation of human milk fat substitutes
title_short Progress and perspectives of enzymatic preparation of human milk fat substitutes
title_sort progress and perspectives of enzymatic preparation of human milk fat substitutes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9635142/
https://www.ncbi.nlm.nih.gov/pubmed/36333804
http://dx.doi.org/10.1186/s13068-022-02217-8
work_keys_str_mv AT liuzeqing progressandperspectivesofenzymaticpreparationofhumanmilkfatsubstitutes
AT dailingmei progressandperspectivesofenzymaticpreparationofhumanmilkfatsubstitutes
AT liudehua progressandperspectivesofenzymaticpreparationofhumanmilkfatsubstitutes
AT duwei progressandperspectivesofenzymaticpreparationofhumanmilkfatsubstitutes