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Benzyl butyrate esterification mediated by immobilized lipases: Evaluation of batch and fed-batch reactors to overcome lipase-acid deactivation

2018; Elsevier BV; Volume: 78; Linguagem: Inglês

10.1016/j.procbio.2018.12.029

1873-3298

Alessandra Cristina de Meneses, Amanda Gomes Almeida Sá, Lindomar Alberto Lerin, Marcos L. Corazza, Pedro Henrique Hermes de Araújo, Cláudia Sayer, Débora de Olíveira,

Analytical Chemistry and Chromatography

• Benzyl butyrate synthesis via enzymatic esterification in a solvent-free system. • Enzyme acid deactivation at low acid: alcohol molar ratio. • The excess of alcohol reduces the lipase acid-deactivation. • Fed-batch mode ensures enzyme reusability and process viability. • Novozym 435 present a good performance in the process scale-up. In this work, benzyl butyrate was synthesized for the first time via biotechnological esterification of benzyl alcohol and butyric acid in a solvent-free system (SFS). The synthesis was maximized in batch reactors, considering a low substrates molar ratio of 1:1. Novozym 435, a well-known commercial immobilized lipase ( Candida antarctica fraction B - Cal B), was the best biocatalyst in the benzyl butyrate synthesis reaching 80% of conversion, followed by the NS 88011, a new lipase prepared with low-cost non-commercial material (Cal B) (46% of conversion). The butyric acid acted as an enzyme deactivator and the excess of alcohol played an important role in the performance of the immobilized enzymes. A fed-batch strategy was employed to overcome the drawbacks related to the use of alcohol in excess, and the results showed that the Novozym 435 had the activity preserved over many cycles of esterification . The scale-up of the fed-batch reactor showed that Novozym 435 had a good and viable performance in the benzyl butyrate esterification at a molar ratio of 1:1 and SFS.