Abstract
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 Psychrobacter SC65A.3 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.
Highlights
IntroductionFor drug and cosmetic industries, a cold-active lipase-mediated system [27,28] for the acylation of silybin A/B with proper methyl fatty acid esters [29,30] has been designed to Catalysts 2021, 11, x FOR PEER REVIEW
Silybum marianum is a very effective natural remedy known in the popular consciousness as milk thistle and originates from Southern and Southeastern Europe
A valuable biocatalytic process based on the enzymatic activity of a cold-active lipase fraction was successfully elaborated for silymarin for improved bioavailability
Summary
For drug and cosmetic industries, a cold-active lipase-mediated system [27,28] for the acylation of silybin A/B with proper methyl fatty acid esters [29,30] has been designed to Catalysts 2021, 11, x FOR PEER REVIEW. For the methyl decanoate agent, silybin conversion reached a maximum value of 65%, which is more than three times higher compared to the free lipase biocatalyst. A second observation that correlated with the immobilized lipase biocatalysts (S1 and S3) is given by the increased biocatalytic potential in a constant trend with the increase in the hydrocarbon chain provided by the acylation agent This behavior is obvious for the S3 bio-composite (49, 53, 61, and 64% silybin conversion for methyl decanoate, methyl laurate, methyl myristate, and methyl palmitate, respectively).
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