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Effect of Pichia pastoris host strain on the properties of recombinant Aspergillus niger endoglucanase, EglB

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dc.contributor.authorShazilah Kamaruddinen_US
dc.contributor.authorNor Muhammad Mahadien_US
dc.contributor.authorRosli Md Illiasen_US
dc.contributor.authorOsman Hassanen_US
dc.contributor.authorSuhaila Sulaimanen_US
dc.contributor.authorWilliam Broughtonen_US
dc.contributor.authorIzwan Bharudinen_US
dc.contributor.authorFarah Diba Abu Bakaren_US
dc.contributor.authorAbdul Munir Abdul Muraden_US
dc.date.accessioned2024-05-28T03:36:18Z
dc.date.available2024-05-28T03:36:18Z
dc.date.issued2018
dc.descriptionMalaysian Journal of Microbiology, Vol 14(6) Special Issue 2018, pp. 554-562en_US
dc.description.abstractAims: The methylotrophic yeast Pichia pastoris is widely used to express foreign proteins fused to secretion signals. As the effect of the expression host on the final protein product is unclear, we compared the properties of an endoglucanase (eglB of Aspergillus niger) expressed in two different P. pastoris strains. Methodology and results: Full-length cDNA encoding endoglucanase of A. niger strain ATCC10574 was isolated and expressed in P. pastoris X33 (the methanol utilisation plus phenotype, Mut+) and P. pastoris GS115 (slow methanol utilisation, MutS). EglB-GS115 showed the highest activity and stability at 60 °C while EglB-X33 was most active at 50 °C. EglB-X33 was active towards other substrates such as arabinogalactan, guar gum and locust bean gum besides its specific substrate, carboxymethyl cellulose (CMC). However, EglB-GS115 was only active on CMC. The affinity of EglB-X33 towards CMC (Km = 7.5 mg.mL-1 and specific activity 658 U.mg-1) was higher than that of EglB-GS115 (Km = 11.57 mg.mL-1, specific activity 144 U.mg-1). Conclusion, significance and impact of study: Although eglB was cloned in the same expression vector (pPICZαC), two different characteristics of enzymes were recovered from the supernatant of the different hosts. Thus, expression of recombinant enzyme in different P. pastoris strains greatly affects the physical structure and biochemical properties of the enzyme. Keywords: cellulase, endoglucanase, glycosylation, methanol utilisation phenotype, recombinant enzymeen_US
dc.identifier.doi10.21161/mjm.1461814
dc.identifier.epage562
dc.identifier.issn1823-8262
dc.identifier.issue6
dc.identifier.other2461-10
dc.identifier.spage554
dc.identifier.urihttp://mjm.usm.my/index.php?r=cms/entry/view&id=2205&slug=Effect-of-Pichia-pastoris-host-strain-on-the-properties-of-recombinant-Aspergillus-niger-endoglucanase%2C-EglB
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/4780
dc.identifier.volume14
dc.language.isoenen_US
dc.publisherMalaysian Society for Microbiologyen_US
dc.relation.ispartofMalaysian Journal of Microbiologyen_US
dc.subjectcellulase,en_US
dc.subjectendoglucanase,en_US
dc.subjectglycosylation,en_US
dc.subjectmethanol utilisation phenotype,en_US
dc.subjectrecombinant enzymeen_US
dc.titleEffect of Pichia pastoris host strain on the properties of recombinant Aspergillus niger endoglucanase, EglBen_US
dc.typeArticleen_US
dspace.entity.typePublication

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