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Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.

ABSTRACT: Xylan has a main chain consisting of ?-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they are normally more active than the GH10 enzymes on insoluble substrates, because of their smaller size. GH5 endoxylanases accept arabinose substituents in several subsites and require it in the -?1 subsite. This specificity makes the GH5 endoxylanases very useful for degradation of highly arabinose-substituted xylans and for the selective production of arabinoxylooligosaccharides, without formation of unsubstituted xylooligosaccharides. The GH30 endoxylanases have a related type of specificity in that they require a uronic acid substituent in the -?2 subsite, which makes them very useful for the production of uronic acid substituted oligosaccharides. The ability of dietary xylooligosaccharides to function as prebiotics in humans is governed by their substitution patterns. Endoxylanases are thus excellent tools to tailor prebiotic oligosaccharides to stimulate various types of intestinal bacteria and to cause fermentation in different parts of the gastrointestinal tract. Continuously increasing knowledge on the function of the gut microbiota and discoveries of novel endoxylanases increase the possibilities to achieve health-promoting effects.

SUBMITTER: Nordberg Karlsson E

PROVIDER: S-EPMC6208967 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.

Nordberg Karlsson Eva E Schmitz Eva E Linares-Pastén Javier A JA Adlercreutz Patrick P

Applied microbiology and biotechnology 20180908 21

Xylan has a main chain consisting of β-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they a ...[more]

PMID: 30196329

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Project description:BackgroundCorn arabinoxylan (AX) is a complicated and multibranched antinutritional factor, thereby proving the use of endo-xylanase (EX) to be marginally valid. This study focused on specific types of AX-degrading enzymes (ADEs) to exert the synergy of debranching enzymes and track the prebiotic potential of enzymatic hydrolysates. This study investigated the effects of ADEs on the growth performance, intestinal histomorphology, absorption functions, changes in polysaccharide components, fermentation, and gut microbiota of broiler chickens. Five hundred seventy-six five-day-old Arbor Acres male broiler chickens were randomly allocated into eight treatments with six replicates each. Corn basal diets supplemented with or without enzymes were fed for a 21-day period, specifically including EX, its compatible use with arabinofuranosidase (EXA) or ferulic acid esterase (EXF), and compound groups with the above three enzymes (XAF).ResultsSpecific ADEs stimulated the jejunal villus height and goblet cell number and evidently decreased the crypt depth (P < 0.05), while the ratio of ileal villus height to crypt depth was significantly increased in EXF (P < 0.05). Maltase activities of ileal mucosa in XAF groups were extremely enhanced (P < 0.01), and EX boosted the activity of Na+-K+ ATPase in the small intestine (P < 0.01). The insoluble AX concentrations comparatively lessened, thereby notably raising the sundry xylooligosaccharide (XOS) yield in the ileal chyme (P < 0.05), which was dominant in xylobiose and xylotriose. Improvements in the abundance and diversity of ileal microbial communities within the EXA, EXF, and XAF treatments were observed (P < 0.05). Positive correlations between microbiota and XOS were revealed, with xylobiose and xylotriose being critical for ten beneficial bacteria (P < 0.05). EXF increased the BWG and FCR of broiler chickens in this phase (P < 0.05), which was attributed to the thriving networks modified by Lactobacillus. The intracecal contents of acetic acid, butyric acid, and propionic acid were greatly enhanced in most ADE groups, such as EXF (P < 0.05).ConclusionsDebranching enzymes appreciably targeted corn AX to release prebiotic XOS in the posterior ileum and facilitated intracaecal fermentation. It was beneficial for improving gut development, digestion and absorption and modulating the microflora to promote the early performance of broiler chickens.

Dataset Information

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.

Publications

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.

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