Jet cutter technique as a tool to achieve high lipase hydrolytic activity

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.contributorItal-
Autor(es): dc.creatorAlmeida, Francisco Lucas Chaves-
Autor(es): dc.creatorSilveira, Mariana Pereira-
Autor(es): dc.creatorAlvim, Izabela Dutra-
Autor(es): dc.creatorda Costa, Talles Barcelos-
Autor(es): dc.creatorda Silva, Thiago Lopes-
Autor(es): dc.creatorVieira, Melissa Gurgel Adeodato-
Autor(es): dc.creatorPrata, Ana Silvia-
Autor(es): dc.creatorForte, Marcus Bruno Soares-
Data de aceite: dc.date.accessioned2025-08-21T19:34:34Z-
Data de disponibilização: dc.date.available2025-08-21T19:34:34Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2022-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.fbp.2022.12.001-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/249013-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/249013-
Descrição: dc.descriptionLipase immobilization has been widely studied because it allows for enzyme reuse and provides more assertive control over the catalytic process. This study aimed to evaluate the effect of bead size on the performance of entrapped lipase. Eversa® Transform 2.0 was immobilized on calcium alginate beads by jet cutting and dripping. Beads produced by jet cutting were small (D[3,4] = 803.36 ± 16.9 µm) and had a relatively narrow size distribution (span of 0.79). Beads obtained by extrusion dripping measured 2459.98 ± 15.6 µm and had a span of 0.45. Infrared spectroscopy and microscopic analysis confirmed the presence of lipase in both types of beads. Lipase showed high hydrolytic activity in its free form (15,000 U g−1). Immobilization in calcium alginate was effective but decreased recovered enzyme activity. The porosity of loaded beads varied with size. The high surface area (5.46 vs 3.13 m2 g−1) and porosity (76.33% vs 21.65%) of beads produced by jet cutting, as compared with those produced by dripping, favored enzyme activity (3000 vs 1500 U g−1 protein). The results indicate that facilitated mass transfer is an important factor in the development of immobilized enzymes.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionInterinstitutional Graduate Program in Bioenergy (USP/UNICAMP/UNESP), Rua Cora Coralina, 330, Cidade Universitária, São Paulo-
Descrição: dc.descriptionMetabolic and Bioprocess Engineering Laboratory Department of Food Engineering and Technology School of Food Engineering University of Campinas, São Paulo-
Descrição: dc.descriptionLaboratory of Food Innovation Department of Food Engineering and Technology Faculty of Food Engineering University of Campinas, São Paulo-
Descrição: dc.descriptionCereal and Chocolate Technology Center Cereal Chocotec Institute of Food Technology Ital, São Paulo-
Descrição: dc.descriptionLaboratory of Engineering and Environmental Processes Department of Process and Product Design School of Chemical Engineering University of Campinas, São Paulo-
Descrição: dc.descriptionInterinstitutional Graduate Program in Bioenergy (USP/UNICAMP/UNESP), Rua Cora Coralina, 330, Cidade Universitária, São Paulo-
Descrição: dc.descriptionCAPES: 001-
Descrição: dc.descriptionFAPESP: 2019-03399-8-
Formato: dc.format189-199-
Idioma: dc.languageen-
Relação: dc.relationFood and Bioproducts Processing-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEntrapment-
Palavras-chave: dc.subjectEnzyme immobilization-
Palavras-chave: dc.subjectEversa-
Palavras-chave: dc.subjectTransform 2.0-
Título: dc.titleJet cutter technique as a tool to achieve high lipase hydrolytic activity-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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