Influence of a family 29 carbohydrate binding module on the recombinant production of galactose oxidase in Pichia pastoris

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en Mollerup, Filip Master, Emma 2017-05-11T09:09:21Z 2017-05-11T09:09:21Z 2016-03-01
dc.identifier.citation Mollerup , F & Master , E 2016 , ' Influence of a family 29 carbohydrate binding module on the recombinant production of galactose oxidase in Pichia pastoris ' Data in Brief , vol 6 , pp. 176-183 . DOI: 10.1016/j.dib.2015.11.032 en
dc.identifier.issn 2352-3409
dc.identifier.other PURE UUID: d984035b-7539-4ad5-b74a-f925ed7903df
dc.identifier.other PURE ITEMURL:
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dc.description.abstract Herein, we report the extracellular expression of carbohydrate active fusion enzymes in Pichia pastoris. Particularly, CBM29-1-2 from Piromyces equi was separately fused to the N- and C-terminus of galactose 6-oxidase (GaO, D-galactose: oxygen 6-oxidoreductase, EC, CAZy family AA5) from Fusarium graminearum, generating CBM29-GaO and GaO-CBM29, respectively. P. pastoris was transformed with expression vectors encoding GaO, CBM29-GaO and GaO-CBM29, and the fusion proteins were expressed in both shake-flask and 2L bioreactor systems. Volumetric production yields and specific GaO activity increased when expression was performed in a bioreactor system compared to shake-flask cultivation. This was observed for both CBM29-GaO and GaO-CBM29, and is consistent with previous reports of GaO expression in P. pastoris (Spadiut et al., 2010; Anasontzis et al., 2014) [1,2]. Fusion of CBM29 to the C-terminal of GaO (GaO-CBM29) resulted in a stable uniform protein at the expected calculated size (107 kDa) when analyzed with SDS-PAGE. By comparison, the expression of the N-terminal fusion protein (CBM29-GaO) was low, and two truncated versions of CBM29-GaO were coexpressed with the full-sized protein. Despite differences in protein yield, the specific GaO activity on galactose was not affected by CBM29 fusion to either the N- or C-terminus of the enzyme. A detailed description of the catalytic and physiochemical properties of CBM29-GaO and GaO-CBM29 is available in the parent publication (Mollerup et al., 2015) [3]. en
dc.format.extent 8
dc.format.extent 176-183
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation info:eu-repo/grantAgreement/EC/H2020/33947/EU//BHIVE
dc.relation.ispartofseries Data in Brief en
dc.relation.ispartofseries Volume 6 en
dc.rights openAccess en
dc.subject.other General en
dc.subject.other Education en
dc.subject.other 215 Chemical engineering en
dc.title Influence of a family 29 carbohydrate binding module on the recombinant production of galactose oxidase in Pichia pastoris en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department Department of Biotechnology and Chemical Technology
dc.contributor.department Department of Bioproducts and Biosystems en
dc.subject.keyword Carbohydrate binding modules
dc.subject.keyword CBM29
dc.subject.keyword Enzyme fusion
dc.subject.keyword Fermentation
dc.subject.keyword Galactose oxidase
dc.subject.keyword Protein production
dc.subject.keyword Protein purification
dc.subject.keyword General
dc.subject.keyword Education
dc.subject.keyword 215 Chemical engineering
dc.identifier.urn URN:NBN:fi:aalto-201705114272
dc.identifier.doi 10.1016/j.dib.2015.11.032
dc.type.version publishedVersion

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