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Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

dc.contributor.authorMachado, Suellen
dc.contributor.authorFeitosa, Valker
dc.contributor.authorPillaca-Pullo, Omar
dc.contributor.authorLario, Luciana
dc.contributor.authorSette, Lara [UNESP]
dc.contributor.authorPessoa, Adalberto
dc.contributor.authorAlves, Harley
dc.contributor.institutionUniversidade Estadual da Paraíba (UEPB)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal do Pará (UFPA)
dc.contributor.institutionUniversidade Federal de Viçosa (UFV)
dc.contributor.institutionUniversidad Privada Norbert Wiener
dc.contributor.institutionPontificia Universidad Católica Argentina (UCA)
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2023-07-29T12:54:53Z
dc.date.available2023-07-29T12:54:53Z
dc.date.issued2022-11-01
dc.description.abstractMicrobial proteases, especially aspartic proteases, are an essential group of enzymes produced from different microorganisms. Microbial proteases have several applications, mainly in the food, beverage, cosmetic, and pharmaceutical industries, due to their efficiency in the processing and in the manufacturing stages. The yeast Rhodotorula mucilaginosa CBMAI 1528 was isolated from the Antarctic environment and was previously reported to have higher extracellular aspartic protease production. In addition, advances in the operational conditions of bioreactors for enzyme production are important to reduce the gap associated with scaling−up processes. This is the first study that evaluates the influence of oxygen transference (kLa) on the protease production of R. mucilaginosa yeast. To that end, batch cultures were created in a stirred tank bioreactor using Sabouraud dextrose broth at 25 °C for 72 h under kLa values from 18 to 135 h−1. The results show that kLa (121 h−1) obtained at 500 rpm and 1.5 vvm plays an important role in protease production (124.9 U/mL) and productivity (6.784 U/L.h) as well as biomass (10.4 g/L), μmax (0.14 h−1) and Yx/s (0.484 g/g). In conclusion, R. mucilaginosa showed high yield production in aerobic culture with the efficiency of protease expression and secretion influenced by kLa. In this sense, our results could be used for further industrial investment.en
dc.description.affiliationDepartamento de Farmácia Programa de Pós-Graduação em Ciências Farmacêuticas Universidade Estadual da Paraíba (UEPB)
dc.description.affiliationDepartamento de Tecnologia Bioquímico-Farmacêutica Universidade de São Paulo (USP)
dc.description.affiliationFaculdade de Biomedicina Instituto de Ciências Biológicas Universidade Federal do Pará (UFPA)
dc.description.affiliationDepartamento de Medicina e Enfermagem Universidade Federal de Viçosa (UFV)
dc.description.affiliationCentro de Investigación en Biodiversidad para la Salud Universidad Privada Norbert Wiener
dc.description.affiliationInstituto de Ingeniería Ambiental Química y Biotecnología Aplicada (INGEBIO) Facultad de Química e Ingeniería del Rosario Pontificia Universidad Católica Argentina (UCA)
dc.description.affiliationDepartamento de Biologia Geral e Aplicada Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
dc.description.affiliationUnespDepartamento de Biologia Geral e Aplicada Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
dc.identifierhttp://dx.doi.org/10.3390/bioengineering9110694
dc.identifier.citationBioengineering, v. 9, n. 11, 2022.
dc.identifier.doi10.3390/bioengineering9110694
dc.identifier.issn2306-5354
dc.identifier.scopus2-s2.0-85149473921
dc.identifier.urihttp://hdl.handle.net/11449/246948
dc.language.isoeng
dc.relation.ispartofBioengineering
dc.sourceScopus
dc.subjectbioreactor
dc.subjectextremophilic
dc.subjectoxygen transference
dc.subjectproteinase
dc.subjectproteolytic
dc.subjectpsychrophilic
dc.titleEffects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactoren
dc.typeArtigo
dspace.entity.typePublication
unesp.author.orcid0000-0001-5608-1768[1]
unesp.author.orcid0000-0001-8205-3883[3]
unesp.author.orcid0000-0003-3046-9611[4]
unesp.author.orcid0000-0002-5268-8690[6]
unesp.author.orcid0000-0002-7734-6857[7]

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