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

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dc.contributor.authorAlmeida, Francisco Lucas Chaves [UNESP]
dc.contributor.authorSilveira, Mariana Pereira
dc.contributor.authorAlvim, Izabela Dutra
dc.contributor.authorda Costa, Talles Barcelos
dc.contributor.authorda Silva, Thiago Lopes
dc.contributor.authorVieira, Melissa Gurgel Adeodato
dc.contributor.authorPrata, Ana Silvia
dc.contributor.authorForte, Marcus Bruno Soares [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionItal
dc.date.accessioned2023-07-29T13:59:58Z
dc.date.available2023-07-29T13:59:58Z
dc.date.issued2023-01-01
dc.description.abstractLipase 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.en
dc.description.affiliationInterinstitutional Graduate Program in Bioenergy (USP/UNICAMP/UNESP), Rua Cora Coralina, 330, Cidade Universitária, São Paulo
dc.description.affiliationMetabolic and Bioprocess Engineering Laboratory Department of Food Engineering and Technology School of Food Engineering University of Campinas, São Paulo
dc.description.affiliationLaboratory of Food Innovation Department of Food Engineering and Technology Faculty of Food Engineering University of Campinas, São Paulo
dc.description.affiliationCereal and Chocolate Technology Center Cereal Chocotec Institute of Food Technology Ital, São Paulo
dc.description.affiliationLaboratory of Engineering and Environmental Processes Department of Process and Product Design School of Chemical Engineering University of Campinas, São Paulo
dc.description.affiliationUnespInterinstitutional Graduate Program in Bioenergy (USP/UNICAMP/UNESP), Rua Cora Coralina, 330, Cidade Universitária, São Paulo
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdCAPES: 001
dc.description.sponsorshipIdFAPESP: 2019-03399-8
dc.format.extent189-199
dc.identifierhttp://dx.doi.org/10.1016/j.fbp.2022.12.001
dc.identifier.citationFood and Bioproducts Processing, v. 137, p. 189-199.
dc.identifier.doi10.1016/j.fbp.2022.12.001
dc.identifier.issn0960-3085
dc.identifier.scopus2-s2.0-85143877688
dc.identifier.urihttp://hdl.handle.net/11449/249013
dc.language.isoeng
dc.relation.ispartofFood and Bioproducts Processing
dc.sourceScopus
dc.subjectEntrapment
dc.subjectEnzyme immobilization
dc.subjectEversa
dc.subjectTransform 2.0
dc.titleJet cutter technique as a tool to achieve high lipase hydrolytic activityen
dc.typeArtigo
unesp.departmentDesign - FAACpt

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Bauru - FAAC - Faculdade de Arquitetura, Artes, Comunicação e Design