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Sökning: onr:"swepub:oai:lup.lub.lu.se:25e86bb3-1109-47ae-9d48-a87f56c20a5f" > Carbohydrate-bindin...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004252naa a2200433 4500
001oai:lup.lub.lu.se:25e86bb3-1109-47ae-9d48-a87f56c20a5f
003SwePub
008181114s2000 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/25e86bb3-1109-47ae-9d48-a87f56c20a5f2 URI
024a https://doi.org/10.1042/0264-6021:34500532 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Abou Hachem, Maheru Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-mah
2451 0a Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase : Cloning, expression and binding studies
264 1b Portland Press Ltd.c 2000
300 a 8 s.
520 a The two N-terminally repeated carbohydrate-binding modules (CBM4-1 and CBM4-2) encoded by xyn10A from Rhodothermus marinus were produced in Escherichia coli and purified by affinity chromatography. Binding assays to insoluble polysaccharides showed binding to insoluble xylan and to phosphoric-acid-swollen cellulose but not to Avicel or crystalline cellulose. Binding to insoluble substrates was significantly enhanced by the presence of Na+ and Ca2+ ions. The binding affinities for soluble polysaccharides were tested by affinity electrophoresis; strong binding occurred with different xylans and β-glucan. CBM4-2 displayed a somewhat higher binding affinity than CBM4-1 for both soluble and insoluble substrates but both had similar specificities. Binding to short oligosaccharides was measured by NMR; both modules bound with similar affinities. The binding of the modules was shown to be dominated by enthalpic forces. The binding modules did not contribute with any significant synergistic effects on xylan hydrolysis when incubated with a Xyn10A catalytic module. This is the first report of family 4 CBMs with affinity for both insoluble xylan and amorphous cellulose.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a CBD
653 a Hemicellulose binding
653 a Modular proteins
653 a Xyn10A
700a Nordberg Karlsson, Evau Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-eno
700a Bartonek-Roxå, Evau Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)med-ebx
700a Raghothama, Srinivasraou University of Sheffield4 aut
700a Simpson, Peter J.u University of Sheffield4 aut
700a Gilbert, Harry J.u University of Newcastle upon Tyne4 aut
700a Williamson, Michael P.u University of Sheffield4 aut
700a Holst, Olleu Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-oho
710a Bioteknikb Centrum för tillämpade biovetenskaper4 org
773t Biochemical Journald : Portland Press Ltd.g 345:1, s. 53-60q 345:1<53-60x 0264-6021
856u http://dx.doi.org/10.1042/0264-6021:3450053y FULLTEXT
856u https://europepmc.org/articles/pmc1220729?pdf=render
8564 8u https://lup.lub.lu.se/record/25e86bb3-1109-47ae-9d48-a87f56c20a5f
8564 8u https://doi.org/10.1042/0264-6021:3450053

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