Matches in SemOpenAlex for { <https://semopenalex.org/work/W4297141779> ?p ?o ?g. }
Showing items 1 to 96 of
96
with 100 items per page.
- W4297141779 endingPage "110136" @default.
- W4297141779 startingPage "110136" @default.
- W4297141779 abstract "Phytases are valuable industrial enzymes widely used in animal feed production, and when expressed in yeast, they undergo glycosylation. Herein, heterologous expression in Pichia pastoris and biochemical characterisation of glycosylated and deglycosylated forms of a novel phytase from Cronobacter turicensis belonging to the histidine acid phosphatase family were successfully carried out. Mutants with deleted N-glycosylation sites (N136, N171, and N202) were constructed by site-directed mutagenesis and characterised. Deglycosylation greatly changed the resistance of phytase to proteolysis, acidic pH, and temperature, but did not significantly affect other biochemical properties. High specific activity (1705 U/mg), Km (173 μM), and Vmax (2778 μmol min-1 mg-1), as well as the optimum temperature (50 °C) and pH (4.5) of the enzyme did not depend on the degree of glycosylation. The degree of change in resistance of phytase depended on the position of the N-glycosylation site on the protein globule. The removal of glycan at the N202 site located in the highly flexible region of the protein had the greatest effect on the enzyme characteristics and led to a decrease in resistance of phytase to pepsin and trypsin by 73% and 87%, respectively. Conversely, the glycosylated enzyme exhibited strong resistance to pepsin, trypsin, and acidic pH, and increased thermostability. It has been shown that N-glycosylation occurring in P. pastoris served as a powerful tool for improving the biochemical properties of recombinant phytase and made it promising for use as an animal feed additive." @default.
- W4297141779 created "2022-09-27" @default.
- W4297141779 creator A5011548231 @default.
- W4297141779 creator A5025084553 @default.
- W4297141779 creator A5063009525 @default.
- W4297141779 date "2023-01-01" @default.
- W4297141779 modified "2023-09-29" @default.
- W4297141779 title "Biochemical characterisation of glycosylated and deglycosylated forms of phytase from Cronobacter turicensis expressed in Pichia pastoris" @default.
- W4297141779 cites W1970107480 @default.
- W4297141779 cites W1993028355 @default.
- W4297141779 cites W1993522365 @default.
- W4297141779 cites W1994110806 @default.
- W4297141779 cites W1998831549 @default.
- W4297141779 cites W1999421182 @default.
- W4297141779 cites W2023821590 @default.
- W4297141779 cites W2038067388 @default.
- W4297141779 cites W2042993286 @default.
- W4297141779 cites W2048677617 @default.
- W4297141779 cites W2056223468 @default.
- W4297141779 cites W2056728361 @default.
- W4297141779 cites W2060138808 @default.
- W4297141779 cites W2067875508 @default.
- W4297141779 cites W2071178103 @default.
- W4297141779 cites W2088514673 @default.
- W4297141779 cites W2123670772 @default.
- W4297141779 cites W2124707779 @default.
- W4297141779 cites W2125683533 @default.
- W4297141779 cites W2142505433 @default.
- W4297141779 cites W2167830808 @default.
- W4297141779 cites W2203174641 @default.
- W4297141779 cites W2731464816 @default.
- W4297141779 cites W2790313939 @default.
- W4297141779 cites W2884419343 @default.
- W4297141779 cites W2890914945 @default.
- W4297141779 cites W2916797734 @default.
- W4297141779 cites W2955404043 @default.
- W4297141779 cites W3045631058 @default.
- W4297141779 doi "https://doi.org/10.1016/j.enzmictec.2022.110136" @default.
- W4297141779 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36195031" @default.
- W4297141779 hasPublicationYear "2023" @default.
- W4297141779 type Work @default.
- W4297141779 citedByCount "2" @default.
- W4297141779 countsByYear W42971417792023 @default.
- W4297141779 crossrefType "journal-article" @default.
- W4297141779 hasAuthorship W4297141779A5011548231 @default.
- W4297141779 hasAuthorship W4297141779A5025084553 @default.
- W4297141779 hasAuthorship W4297141779A5063009525 @default.
- W4297141779 hasConcept C104317684 @default.
- W4297141779 hasConcept C108625454 @default.
- W4297141779 hasConcept C109551439 @default.
- W4297141779 hasConcept C181199279 @default.
- W4297141779 hasConcept C185592680 @default.
- W4297141779 hasConcept C206212055 @default.
- W4297141779 hasConcept C2777313579 @default.
- W4297141779 hasConcept C2780340462 @default.
- W4297141779 hasConcept C2781216036 @default.
- W4297141779 hasConcept C2781372317 @default.
- W4297141779 hasConcept C30324644 @default.
- W4297141779 hasConcept C40767141 @default.
- W4297141779 hasConcept C55493867 @default.
- W4297141779 hasConcept C86803240 @default.
- W4297141779 hasConceptScore W4297141779C104317684 @default.
- W4297141779 hasConceptScore W4297141779C108625454 @default.
- W4297141779 hasConceptScore W4297141779C109551439 @default.
- W4297141779 hasConceptScore W4297141779C181199279 @default.
- W4297141779 hasConceptScore W4297141779C185592680 @default.
- W4297141779 hasConceptScore W4297141779C206212055 @default.
- W4297141779 hasConceptScore W4297141779C2777313579 @default.
- W4297141779 hasConceptScore W4297141779C2780340462 @default.
- W4297141779 hasConceptScore W4297141779C2781216036 @default.
- W4297141779 hasConceptScore W4297141779C2781372317 @default.
- W4297141779 hasConceptScore W4297141779C30324644 @default.
- W4297141779 hasConceptScore W4297141779C40767141 @default.
- W4297141779 hasConceptScore W4297141779C55493867 @default.
- W4297141779 hasConceptScore W4297141779C86803240 @default.
- W4297141779 hasFunder F4320321912 @default.
- W4297141779 hasLocation W42971417791 @default.
- W4297141779 hasLocation W42971417792 @default.
- W4297141779 hasOpenAccess W4297141779 @default.
- W4297141779 hasPrimaryLocation W42971417791 @default.
- W4297141779 hasRelatedWork W1998831549 @default.
- W4297141779 hasRelatedWork W2023763937 @default.
- W4297141779 hasRelatedWork W2057984012 @default.
- W4297141779 hasRelatedWork W2071178103 @default.
- W4297141779 hasRelatedWork W2083040603 @default.
- W4297141779 hasRelatedWork W2147989907 @default.
- W4297141779 hasRelatedWork W2968881857 @default.
- W4297141779 hasRelatedWork W3147162310 @default.
- W4297141779 hasRelatedWork W4297141779 @default.
- W4297141779 hasRelatedWork W4315865859 @default.
- W4297141779 hasVolume "162" @default.
- W4297141779 isParatext "false" @default.
- W4297141779 isRetracted "false" @default.
- W4297141779 workType "article" @default.