{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nilpa P"],"funding":["Universiti Teknologi Malaysia","Taif University"],"pagination":["e0265969"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8975109"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(4)"],"pubmed_abstract":["The tissue of insects, pests, and fungi has a chitin layer followed by protein in the cell membrane. The complete biodegradation of chitin and protein-present in the waste requires the action of two enzymes, namely chitinase, and protease. Combining chitinase and protease in a single protein/enzyme will serve as a bifunctional enzyme that can efficiently degrade the chitin and protein-rich biomass. The present study was aimed to fuse these two enzymes to produce a single protein and study the kinetics of the recombinant fusion protein. A chitinase and alkaline protease genes were isolated, cloned, and expressed successfully as a fusion product in heterologous host Escherichia coli. The two native genes were successfully fused in E.coli by using flexible glycine-serine (G4S)2 linker (GGGGS,"],"journal":["PloS one"],"pubmed_title":["Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein."],"pmcid":["PMC8975109"],"funding_grant_id":["RJ130000.7609.4C359 and RJ130000.7609.4C336","TURSP-2020/208"],"pubmed_authors":["Sayyed RZ","Alhazmi A","Chintan K","El Enshasy H","El Adawi H","Nilpa P","Almalki AH","Haque S"],"additional_accession":[]},"is_claimable":false,"name":"Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein.","description":"The tissue of insects, pests, and fungi has a chitin layer followed by protein in the cell membrane. The complete biodegradation of chitin and protein-present in the waste requires the action of two enzymes, namely chitinase, and protease. Combining chitinase and protease in a single protein/enzyme will serve as a bifunctional enzyme that can efficiently degrade the chitin and protein-rich biomass. The present study was aimed to fuse these two enzymes to produce a single protein and study the kinetics of the recombinant fusion protein. A chitinase and alkaline protease genes were isolated, cloned, and expressed successfully as a fusion product in heterologous host Escherichia coli. The two native genes were successfully fused in E.coli by using flexible glycine-serine (G4S)2 linker (GGGGS,","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-31T01:04:19.605Z","creation":"2025-04-04T11:31:50.777Z"},"accession":"S-EPMC8975109","cross_references":{"pubmed":["35363796"],"doi":["10.1371/journal.pone.0265969"]}}