Characterization of thermostable carboxypeptidase from high-altitude hot spring metagenome

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Autor(es): dc.contributorLovely Professional University-
Autor(es): dc.contributorKing Saud University-
Autor(es): dc.contributorJiangsu University-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorBrazil University-
Autor(es): dc.creatorWani, Atif Khurshid-
Autor(es): dc.creatorChopra, Chirag-
Autor(es): dc.creatorAnsari, Mushtaq Ahmad-
Autor(es): dc.creatorDar, Mudasir A.-
Autor(es): dc.creatorAmérico-Pinheiro, Juliana Heloisa Pinê-
Autor(es): dc.creatorSingh, Reena-
Data de aceite: dc.date.accessioned2025-08-21T16:29:07Z-
Data de disponibilização: dc.date.available2025-08-21T16:29:07Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-09-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2024.133974-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/298134-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/298134-
Descrição: dc.descriptionThis study explored the metagenome of the Pir Panjal Hot Spring (PPHS) to identify thermostable hydrolases. The carboxypeptidase (CarP) gene was successfully amplified and cloned into Escherichia coli DH5-α cells, followed by expression in E. coli BL21-DE3 cells. The CarP enzyme was comprehensively characterized in vitro. Sequencing analysis revealed an open reading frame encoding a functional protein of 504 amino acids, with a molecular weight of 58.65 kDa and an isoelectric point of 4.81. The CarP protein was purified using Ni-His affinity chromatography, and the experimental molecular weight matched in silico predictions. The enzyme exhibited significant thermostability and alkaliphilic properties, with optimal activity at 70 °C and pH 10.0. Additionally, the presence of Zn+2 ions at concentrations of 5 and 10 mmol/L enhanced protease activity by 1.4 and 1.5-fold, respectively. This study reports the discovery of a novel, multifunctional, and thermostable CarP from hot-spring metagenomes. The enzyme's stability against high temperatures, metal ions, surfactants, and inhibitors, along with its specific substrate interactions, highlights its potential for various biotechnological applications.-
Descrição: dc.descriptionKing Saud University-
Descrição: dc.descriptionSchool of Bioengineering and Biosciences Lovely Professional University, Punjab-
Descrição: dc.descriptionDepartment of Pharmacology and Toxicology College of Pharmacy King Saud University-
Descrição: dc.descriptionSchool of the Environment and Safety Engineering Biofuels Institute Jiangsu University-
Descrição: dc.descriptionSão Paulo State University (UNESP) School of Agricultural Sciences Botucatu Department of Forest Science Soils and Environment, Ave. Universitária, 3780, SP-
Descrição: dc.descriptionGraduate Program in Environmental Sciences Brazil University, Street Carolina Fonseca, 584, SP-
Descrição: dc.descriptionSão Paulo State University (UNESP) School of Agricultural Sciences Botucatu Department of Forest Science Soils and Environment, Ave. Universitária, 3780, SP-
Descrição: dc.descriptionKing Saud University: RSPD2024R996-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Biological Macromolecules-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEnzymes-
Palavras-chave: dc.subjectHydrolases-
Palavras-chave: dc.subjectMetagenomics-
Palavras-chave: dc.subjectProtease-
Palavras-chave: dc.subjectThermostable-
Título: dc.titleCharacterization of thermostable carboxypeptidase from high-altitude hot spring metagenome-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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