Influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en Mollerup, Filip Parikka, Kirsti Vuong, Thu V. Tenkanen, Maija Master, Emma 2019-01-14T09:19:12Z 2019-01-14T09:19:12Z 2016-02-01
dc.identifier.citation Mollerup , F , Parikka , K , Vuong , T V , Tenkanen , M & Master , E 2016 , ' Influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum ' , BIOCHIMICA ET BIOPHYSICA ACTA: GENERAL SUBJECTS , vol. 1860 , no. 2 , pp. 354-362 . en
dc.identifier.issn 0304-4165
dc.identifier.other PURE UUID: 18a93add-dc2a-4018-832c-ca4579a4511a
dc.identifier.other PURE ITEMURL:
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dc.description | openaire: EC/H2020/33947/EU//BHIVE
dc.description.abstract Background Galactose oxidase (GaO) selectively oxidizes the primary hydroxyl of galactose to a carbonyl, facilitating targeted chemical derivatization of galactose-containing polysaccharides, leading to renewable polymers with tailored physical and chemical properties. Here we investigate the impact of a family 29 glucomannan binding module on the activity and binding of GaO towards various polysaccharides. Specifically, CBM29-1-2 from Piromyces equi was separately linked to the N- and C-termini of GaO. Results Both GaO-CBM29 and CBM29-GaO were successfully expressed in Pichia pastoris, and demonstrated enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan. The position of the CBM29 fusion affected the enzyme function. Particularly, C-terminal fusion led to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increased by 7.5 and 19.8 times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induced oligomerization of GaO-CBM29. Major conclusions Similar to impacts of cellulose-binding modules associated with cellulolytic enzymes, increased substrate binding impeded the action of GaO fusions on more concentrated preparations of galactomannan, galactoglucomannan and galactoxyloglucan; this was especially true for GaO-CBM29. Given the N-terminal positioning of the native galactose-binding CBM32 in GaO, the varying impacts of N-terminal versus C-terminal fusion of CBM29-1-2 may reflect competing action of neighboring CBMs. General significance This study thoroughly examines and discusses the effects of CBM fusion to non-lignocellulytic enzymes on soluble polysaccharides. Herein kinetics of GaO on galactose containing polysaccharides is presented for the first time. en
dc.format.extent 9
dc.format.extent 354-362
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation info:eu-repo/grantAgreement/EC/H2020/33947/EU//BHIVE
dc.relation.ispartofseries Volume 1860, issue 2 en
dc.rights openAccess en
dc.subject.other Biochemistry en
dc.subject.other Biophysics en
dc.subject.other Molecular Biology en
dc.subject.other 215 Chemical engineering en
dc.title Influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum 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 University of Helsinki
dc.contributor.department University of Toronto
dc.contributor.department Department of Bioproducts and Biosystems en
dc.subject.keyword Carbohydrate binding module
dc.subject.keyword Fusion proteins
dc.subject.keyword Galactoglucomannan
dc.subject.keyword Galactomannan
dc.subject.keyword Galactose oxidase
dc.subject.keyword Galactoxyloglucan
dc.subject.keyword Biochemistry
dc.subject.keyword Biophysics
dc.subject.keyword Molecular Biology
dc.subject.keyword 215 Chemical engineering
dc.identifier.urn URN:NBN:fi:aalto-201901141097
dc.identifier.doi 10.1016/j.bbagen.2015.10.023
dc.type.version acceptedVersion info:eu-repo/date/embargoEnd/2018-02-02

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