A comprehensive review of eclectic approaches to the biological synthesis of vanillin and their application towards the food sector.

Vanillin, a highly regarded flavor compound, has earned widespread recognition for its natural and aromatic qualities, piquing substantial interest in the scientific community. This comprehensive review delves deeply into the intricate world of vanillin synthesis, encompassing a wide spectrum of methodologies, including enzymatic, microbial, and immobilized systems. This investigation provides a thorough analysis of the precursors of vanillin and also offers a comprehensive overview of its transformation through these diverse processes, making it an invaluable resource for researchers and enthusiasts alike. The elucidation of different substrates such as ferulic acid, eugenol, veratraldehyde, vanillic acid, glucovanillin, and C6-C3 phenylpropanoids adds a layer of depth and insight to the understanding of vanillin synthesis. Moreover, this comprehensive review explores the multifaceted applications of vanillin within the food industry. While commonly known as a flavoring agent, vanillin transcends this role by finding extensive use in food preservation and food packaging. The review meticulously examines the remarkable preservative properties of vanillin, providing a profound understanding of its crucial role in the culinary and food science sectors, thus making it an indispensable reference for professionals and researchers in these domains.

Laccase-immobilized on superparamagnetic iron oxide nanoparticles incorporated polymeric ultrafiltration membrane for the removal of toxic pentachlorophenol.

A biocatalytic membrane offers an ideal alternative to the conventional treatment process for the removal of toxic pentachlorophenol (PCP). The limelight of the study is to utilize superparamagnetic iron oxide nanoparticles (SPIONs) incorporated (poly (methyl vinyl ether-alt-maleic acid) (PMVEAMA) and poly (ether - ether) sulfone (PEES)) membrane for immobilization of laccase and its application towards the removal of PCP. In regard to immobilization of Tramates versicolor laccase onto membranes, 5 mM glutaraldehyde with 10 h cross-linking time was employed, yielding 76.92% and 77.96% activity recovery for PEES/PMVEAMA/La and PEES/PMVEAMA/SPIONs/Lac, respectively. In the context of kinetics and stability studies, the immobilized laccase on PEES/PMVEAMA/Lac membrane outperforms the free and PEES/PMVEAMA laccases. At pH 7.0, the free enzyme loses half of its activity, while the immobilized laccases maintained more than 87% of their initial activity even after 480 min. With regard to PCP removal, the removal efficiency of immobilized laccase on the membrane was more than free enzyme. With 100 ppm of PCP, immobilized laccase on PEES/PMVEAMA/SPIONs membrane at pH 4.0 and 50 °C had a removal efficacy of 61.65% in 24 h. Furthermore, to perk up the removal of PCP, the laccase-aided system with mediators was investigated. Amongst, veratryl alcohol displayed 71.04% of PCP removal using immobilized laccase. The reusability of the laccase heightened after immobilization on PEES/PMVEAMA/SPIONs portraying 62.44% of the residual activity with 39.4% of PCP removal even after five cycles. The current investigation reveals the efficacy of the mediator-aided PEES/PMVEAMA/lac membrane system towards removing PCP from the aqueous solution, which can also be proposed for a membrane bioreactor.