Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/46285

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dc.contributor.authorPacheco, Ana Margaridapor
dc.contributor.authorBarroca, Mário Jorge Fariapor
dc.contributor.authorOliveira, Brunopor
dc.contributor.authorVeloso, Paulopor
dc.contributor.authorSantos, Gustavopor
dc.contributor.authorCollins, Tonypor
dc.date.accessioned2017-07-27T10:11:36Z-
dc.date.issued2017-
dc.identifier.urihttps://hdl.handle.net/1822/46285-
dc.description.abstract[Excerpt] Xylanases (EC 3.2.1.8) are glycoside hydrolase enzymes which breakdown the β-1,4 linkages of xylan, one of the most abundant polysaccharide in the cell wall of plants. Xylanases are important industrial enzymes with application in the food, feed and industrial enzymes markets. pXyl is an industrially important psychrophilic family 8 xylanase which is already being commercialized worldwide for baking applications to improve the size, texture and shelf life of baking products. The commercial value of this enzyme is related to its high rate of activity, production of long chain xylo-oligomer products and resistance to xylanase inhibitors. Nevertheless, this enzyme is also characterised by a low stability and activity at acidic pHs which hinders its application in a number of industries. [...]por
dc.language.isoengpor
dc.rightsrestrictedAccesspor
dc.titleDeciphering the role of exposed surface residues in protein stabilitypor
dc.typeconferenceAbstractpor
dc.peerreviewednopor
oaire.citationConferenceDate30/05/2017por
sdum.event.typeconferencepor
oaire.citationConferencePlaceBraga, Portugalpor
oaire.citationTitleI Simpósio em Bioquímica Aplicadapor
dc.description.publicationversioninfo:eu-repo/semantics/publishedVersionpor
Aparece nas coleções:DBio - Comunicações/Communications in Congresses

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