Enzyme synergy for the production of arabinoxylo-oligosaccharides from highly substituted arabinoxylan and evaluation of their prebiotic potential

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Fältnamn	Indikatorer	Metadata
000		05226naa a2200565 4500
001		oai:DiVA.org:kth-282269
003		SwePub
008		201008s2020 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
009		oai:lup.lub.lu.se:41452c18-cd52-467f-838a-38e5db650c44
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-2822692 URI
024	7	a https://doi.org/10.1016/j.lwt.2020.1097622 DOI
024	7	a https://lup.lub.lu.se/record/41452c18-cd52-467f-838a-38e5db650c442 URI
040		a (SwePub)kthd (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Bhattacharya, Abhisheku Lund Univ, Dept Chem, Biochem & Struct Biol, POB 124, S-22100 Lund, Sweden.,Lund University4 aut
245	1 0	a Enzyme synergy for the production of arabinoxylo-oligosaccharides from highly substituted arabinoxylan and evaluation of their prebiotic potential
264	1	b Elsevier BV,c 2020
338		a print2 rdacarrier
500		a QC 20201008
520		a Wheat bran arabinoxylan can be converted by enzymatic hydrolysis into short arabinoxylo-oligosaccharides (AXOS) with prebiotic potential. Alkali extraction of arabinoxylan from wheat-bran offers advantages in terms of yield and results in arabinoxylan with highly-substituted regions which has been a challenge to hydrolyse using endoxylanases. We show that this hurdle can be overcome by selecting an arabinoxylanase that attacks these regions. The yield of AXOS can be increased by enzyme synergy, involving the hydrolysis of some arabinoxylan side groups. Thus, arabinoxylanase (CtXyl5At) from Clostridium thermocellum, belonging to subfamily 34 of glycoside hydrolase (GH) family 5 was investigated pertaining to its specificity for highly-substituted regions in the arabinoxylan-backbone. CtXyl5At preferentially hydrolysed the water-soluble fraction of alkali-extracted arabinoxylan. AXOS with DP 2-4 were determined as major products from CtXyl5At catalyzed hydrolysis. Increase in AXOS yield was observed with enzyme synergy, involving an initial treatment of soluble arabinoxylan with a GH43 alpha-L-arabinofuranosidase from Bifidobacterium adolescentis termed BaAXHd3 (30 degrees C, 6h), followed by hydrolysis with CtXyl5At (50 degrees C, 24h). The prebiotic potential of AXOS was shown by growth analysis using the human gut bacteria Bifidobacterium adolescentis ATCC 15703 and Roseburia hominis DSM 6839. Importantly, AXOS were utilized by the bacteria and short-chain fatty acids were produced.
650	7	a LANTBRUKSVETENSKAPERx Lantbruksvetenskap, skogsbruk och fiskex Livsmedelsvetenskap0 (SwePub)401032 hsv//swe
650	7	a AGRICULTURAL SCIENCESx Agriculture, Forestry and Fisheriesx Food Science0 (SwePub)401032 hsv//eng
650	7	a TEKNIK OCH TEKNOLOGIERx Annan teknikx Livsmedelsteknik0 (SwePub)211012 hsv//swe
650	7	a ENGINEERING AND TECHNOLOGYx Other Engineering and Technologiesx Food Engineering0 (SwePub)211012 hsv//eng
653		a Arabinoxylo-oligosaccharides
653		a Arabinoxylanase
653		a Enzyme synergy
653		a Prebiotics
653		a Probiotics
653		a Arabinoxylanase
653		a Arabinoxylo-oligosaccharides
653		a Enzyme synergy
653		a Prebiotics
653		a Probiotics
700	1	a Ruthes, Andrea C.u KTH Royal Institute of Technology,KTH,Glykovetenskap4 aut0 (Swepub:kth)u1dt04i4
700	1	a Vilaplana, Francisco,d 1979-u KTH Royal Institute of Technology,KTH,Glykovetenskap4 aut0 (Swepub:kth)u173a4yy
700	1	a Karlsson, Eva Nordbergu 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
700	1	a Adlecreutz, Patricku 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-pad
700	1	a Stålbrand, Henriku Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biok-hst
710	2	a Lund Univ, Dept Chem, Biochem & Struct Biol, POB 124, S-22100 Lund, Sweden.b Lund University4 org
773	0	t Lebensmittel-Wissenschaft + Technologied : Elsevier BVg 131q 131x 0023-6438x 1096-1127
856	4	u https://doi.org/10.1016/j.lwt.2020.109762y Fulltext
856	4	u https://doi.org/10.1016/j.lwt.2020.109762
856	4	u http://dx.doi.org/10.1016/j.lwt.2020.109762x freey FULLTEXT
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-282269
856	4 8	u https://doi.org/10.1016/j.lwt.2020.109762
856	4 8	u https://lup.lub.lu.se/record/41452c18-cd52-467f-838a-38e5db650c44

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