Optimization of protease production and sequence analysis of the purified enzyme from the cold adapted yeast Rhodotorula mucilaginosa CBMAI 1528

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Autor(es): dc.contributorUniversidad Nacional de Rosario-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorPontificia Universidad Católica Argentina (UCA)-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversity of Genoa-
Autor(es): dc.creatorLario, Luciana Daniela-
Autor(es): dc.creatorPillaca-Pullo, Omar Santiago-
Autor(es): dc.creatorDurães Sette, Lara [UNESP]-
Autor(es): dc.creatorConverti, Attilio-
Autor(es): dc.creatorCasati, Paula-
Autor(es): dc.creatorSpampinato, Claudia-
Autor(es): dc.creatorPessoa, Adalberto-
Data de aceite: dc.date.accessioned2022-02-22T00:44:19Z-
Data de disponibilização: dc.date.available2022-02-22T00:44:19Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.btre.2020.e00546-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/205433-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/205433-
Descrição: dc.descriptionEnzymes from cold-adapted microorganisms are of high interest to industries due to their high activity at low and mild temperatures, which makes them suitable for their use in several processes that either require a supply of exogenous energy or involve the use of heat labile products. In this work, the protease production by the strain Rhodotorula mucilaginosa CBMAI 1528, previously isolated from the Antarctic continent, was optimized, and the purified enzyme analyzed. It was found that protease production was dependent on culture medium composition and growth temperature, being 20 °C and a culture medium containing both glucose and casein peptone (20 and 10 g/L, respectively) the optimal growing conditions in batch as well as in bioreactor. Moreover, mass spectrometry analysis revealed that the enzyme under study has a 100 % sequence identity with the deduced amino acid sequence of a putative aspartic protease from Rhodotorula sp. JG-1b (protein ID: KWU42276.1). This result was confirmed by the decrease of 95 % proteolytic activity by pepstatin A, a specific inhibitor of aspartic proteases. We propose that the enzyme reported here could be Rodothorulapepsin, a protein characterized in 1972 that did not have an associated sequence to date and has been classified as an orphan enzyme.-
Descrição: dc.descriptionAgencia Nacional de Promoción Científica y Tecnológica-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI) Facultad de Ciencias Bioquímicas y Farmacéuticas Universidad Nacional de Rosario, Suipacha 531-
Descrição: dc.descriptionDepartment of Biochemical and Pharmaceutical Technology School of Pharmaceutical Sciences University of Sao Paulo, Av. Prof. Lineu Prestes, 580-
Descrição: dc.descriptionInstituto de Ingeniería Ambiental Química y Biotecnología Aplicada (INGEBIO) Facultad de Química e Ingeniería del Rosario Pontificia Universidad Católica Argentina (UCA), Av. Pellegrini 3314-
Descrição: dc.descriptionDepartment of General and Applied Biology Institute of Biosciences Sao Paulo State University (UNESP), Av. 24A, 1515-
Descrição: dc.descriptionDepartment of Civil Chemical and Environmental Engineering Pole of Chemical Engineering University of Genoa, Via Opera Pia 15-
Descrição: dc.descriptionDepartment of General and Applied Biology Institute of Biosciences Sao Paulo State University (UNESP), Av. 24A, 1515-
Idioma: dc.languageen-
Relação: dc.relationBiotechnology Reports-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAntarctic yeast-
Palavras-chave: dc.subjectAspartic protease-
Palavras-chave: dc.subjectRodothorulapepsin-
Título: dc.titleOptimization of protease production and sequence analysis of the purified enzyme from the cold adapted yeast Rhodotorula mucilaginosa CBMAI 1528-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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