Cloning, overexpression, purification, characterization and structural modelling of a metabolically active Fe

Autor:	Oladipupo A, Aregbesola, Ajit, Kumar, Mduduzi P, Mokoena, Ademola O, Olaniran
Rok vydání:	2020
Předmět:	Models Molecular Protein Conformation Iron Temperature Gene Expression Hydrogen-Ion Concentration Gas Chromatography-Mass Spectrometry Recombinant Proteins Dioxygenases Enzyme Activation Structure-Activity Relationship Bacillus cereus Amino Acid Sequence Cloning Molecular Phylogeny
Zdroj:	International journal of biological macromolecules. 161
ISSN:	1879-0003
Popis:	2,6-Dichloro-p-hydroquinone (DiCHQ) aromatic-ring cleavage by DiCHQ 1,2-dioxygenase (CpsA) is very crucial for complete transformation of pentachlorophenol (PCP) to 2-chloromaleylacetate in Bacillus cereus AOA-CPS_1 (BcAOA). The 978 bp gene (cpsA) was detected and amplified in the genome of BcAOA; cloned, overexpressed and purified to homogeneity. CpsA showed a single ≅36.9 kDa protein band on SDS-PAGE and exhibited optimum activity at 30 °C and pH 9.0. CpsA was stable between 20 °C and 40 °C, and also retained about 90% of its activity at 60 °C for 120 min. The enzyme retained about 90% activity between pH 9.0 and 11.5 and 60% activity at pH 13.0. CpsA was found to be Fe
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fc84a52bde50507b499460ebdf66c2bc https://pubmed.ncbi.nlm.nih.gov/32512093 Zobrazit plný text záznamu Full Text from ScienceDirect