Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin

Extremophilic biocatalysts represent an enhanced solution in various industrial applications. Integrating enzymes with high catalytic potential at low temperatures into production schemes such as cold-pressed silymarin processing not only brings value to the silymarin recovery from biomass residues,...

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Autores principales:	Giulia Roxana Gheorghita, Victoria Ioana Paun, Simona Neagu, Gabriel-Mihai Maria, Madalin Enache, Cristina Purcarea, Vasile I. Parvulescu, Madalina Tudorache
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	cold-active lipolytic activity lipase immobilization biocatalysis silymarin silybin Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/0f336a9eeb4444b685a13b9278f6ea3f
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spelling	oai:doaj.org-article:0f336a9eeb4444b685a13b9278f6ea3f2021-11-25T17:06:40ZCold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin10.3390/catal111113902073-4344https://doaj.org/article/0f336a9eeb4444b685a13b9278f6ea3f2021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1390https://doaj.org/toc/2073-4344Extremophilic biocatalysts represent an enhanced solution in various industrial applications. Integrating enzymes with high catalytic potential at low temperatures into production schemes such as cold-pressed silymarin processing not only brings value to the silymarin recovery from biomass residues, but also improves its solubility properties for biocatalytic modification. Therefore, a cold-active lipase-mediated biocatalytic system has been developed for silybin acylation with methyl fatty acid esters based on the extracellular protein fractions produced by the psychrophilic bacterial strain <i>Psychrobacter SC65A.3</i> isolated from Scarisoara Ice Cave (Romania). The extracellular production of the lipase fraction was enhanced by 1% olive-oil-enriched culture media. Through multiple immobilization approaches of the cold-active putative lipases (using carbodiimide, aldehyde-hydrazine, or glutaraldehyde coupling), bio-composites (S1–5) with similar or even higher catalytic activity under cold-active conditions (25 °C) have been synthesized by covalent attachment to nano-/micro-sized magnetic or polymeric resin beads. Characterization methods (e.g., FTIR DRIFT, SEM, enzyme activity) strengthen the biocatalysts’ settlement and potential. Thus, the developed immobilized biocatalysts exhibited between 80 and 128% recovery of the catalytic activity for protein loading in the range 90–99% and this led to an immobilization yield up to 89%. The biocatalytic acylation performance reached a maximum of 67% silybin conversion with methyl decanoate acylating agent and nano-support immobilized lipase biocatalyst.Giulia Roxana GheorghitaVictoria Ioana PaunSimona NeaguGabriel-Mihai MariaMadalin EnacheCristina PurcareaVasile I. ParvulescuMadalina TudoracheMDPI AGarticlecold-active lipolytic activitylipase immobilizationbiocatalysissilymarinsilybinChemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1390, p 1390 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	cold-active lipolytic activity lipase immobilization biocatalysis silymarin silybin Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	cold-active lipolytic activity lipase immobilization biocatalysis silymarin silybin Chemical technology TP1-1185 Chemistry QD1-999 Giulia Roxana Gheorghita Victoria Ioana Paun Simona Neagu Gabriel-Mihai Maria Madalin Enache Cristina Purcarea Vasile I. Parvulescu Madalina Tudorache Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
description	Extremophilic biocatalysts represent an enhanced solution in various industrial applications. Integrating enzymes with high catalytic potential at low temperatures into production schemes such as cold-pressed silymarin processing not only brings value to the silymarin recovery from biomass residues, but also improves its solubility properties for biocatalytic modification. Therefore, a cold-active lipase-mediated biocatalytic system has been developed for silybin acylation with methyl fatty acid esters based on the extracellular protein fractions produced by the psychrophilic bacterial strain <i>Psychrobacter SC65A.3</i> isolated from Scarisoara Ice Cave (Romania). The extracellular production of the lipase fraction was enhanced by 1% olive-oil-enriched culture media. Through multiple immobilization approaches of the cold-active putative lipases (using carbodiimide, aldehyde-hydrazine, or glutaraldehyde coupling), bio-composites (S1–5) with similar or even higher catalytic activity under cold-active conditions (25 °C) have been synthesized by covalent attachment to nano-/micro-sized magnetic or polymeric resin beads. Characterization methods (e.g., FTIR DRIFT, SEM, enzyme activity) strengthen the biocatalysts’ settlement and potential. Thus, the developed immobilized biocatalysts exhibited between 80 and 128% recovery of the catalytic activity for protein loading in the range 90–99% and this led to an immobilization yield up to 89%. The biocatalytic acylation performance reached a maximum of 67% silybin conversion with methyl decanoate acylating agent and nano-support immobilized lipase biocatalyst.
format	article
author	Giulia Roxana Gheorghita Victoria Ioana Paun Simona Neagu Gabriel-Mihai Maria Madalin Enache Cristina Purcarea Vasile I. Parvulescu Madalina Tudorache
author_facet	Giulia Roxana Gheorghita Victoria Ioana Paun Simona Neagu Gabriel-Mihai Maria Madalin Enache Cristina Purcarea Vasile I. Parvulescu Madalina Tudorache
author_sort	Giulia Roxana Gheorghita
title	Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
title_short	Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
title_full	Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
title_fullStr	Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
title_full_unstemmed	Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin
title_sort	cold-active lipase-based biocatalysts for silymarin valorization through biocatalytic acylation of silybin
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/0f336a9eeb4444b685a13b9278f6ea3f
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Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin

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