Degradation of complex carbohydrates by Bifidobacterium spp.

Crociani, F.; Alessandrini, Ambra; Mucci, Marta Maria; Biavati, Bruno

doi:10.1016/0168-1605(94)90119-8

Cited by 137 publications

(103 citation statements)

References 9 publications

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“…The two selective tests to differentiate between the species are the presence of f3-glucuronidase and guar fermentation, both of which are positive for Bif. dentium (7,26).…”

Section: Discussionmentioning

confidence: 99%

Degradation of Guar Gum by Intestinal Bacteria

Hartemink

Schoustra

Rombouts

1999

Bioscience Microflora

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Guar gum is widely used in the food industry as a thickening agent. Guar and other galactomannans are ingested as a normal part of the human diet. Guar is completely degraded in the large intestine. Often large amounts of gas are produced. The objective of the study was to determine which species are responsible for the degradation of guar in the GI tract. It was observed that only a limited number of species is able to degrade and ferment guar. Guar degrading strains could be isolated from faecal samples of all volunteers and in 90% of the saliva of volunteers. The main species isolated from humans were Bifidobacterium dentium and Clostridium butyricum. From several samples of animal faeces Streptococcus bovis could be isolated. In addition some strains of Bacteroides ovatus were able to degrade guar to a limited extent. Fermentation resulted in the production of short-chain fatty acids and, when CL butyricum was present, in a large gas production. Competition experiments showed that Cl. butyricum degrades guar faster than both other species under simulated physiological conditions. It was concluded that Cl. butyricum is the main guar degrading species and the causative agent of the gas formation after guar intake.

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“…The two selective tests to differentiate between the species are the presence of f3-glucuronidase and guar fermentation, both of which are positive for Bif. dentium (7,26).…”

Section: Discussionmentioning

confidence: 99%

Degradation of Guar Gum by Intestinal Bacteria

Hartemink

Schoustra

Rombouts

1999

Bioscience Microflora

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Section: Rabbit Caecum Mucin Bacteriamentioning

confidence: 99%

“…B ayliss and Houston (1984) identified some mucin fermenters as members of the Bacteroides genus, other resembled Bifidobacterium sp., Clostridium septicum, and Eubacterium sp. Crociani et al (1994) found that only Bifidobacterium bifidum strains fermented gastric mucin among 29 species of bifidobacteria tested. Mucin fermenters from the digestive tract of herbivores are almost unknown.…”

mentioning

confidence: 99%

Isolation, Identification and Characterization of Rabbit Caecal Mucinolytic Bacteria

Sirotek¹,

Santos²,

Benda³

et al. 2003

Acta Vet. Brno

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Sirotek K., E. Santos, V. Benda, M. Marounek: Isolation, Identification and Characterization of Rabbit Caecal Mucinolytic Bacteria. Acta Vet. Brno 2003, 72: 365-370.The aim of our study was to isolate, identify and characterize mucinolytic bacteria from the rabbit caecum. Two hundred and thirty mucin-grown colonies from the caecal contents of 7 rabbits were examined microscopically after the Gram staining. Gram-negative irregular rods were the most numerous mucinolytic isolates (34.1%), followed by gram-negative cocci and short rods (22.5%), gram-positive rods (17.3%), gram-positive cocci (16.6%) and gram-positive sporeforming rods (9.5%). An attempt was done to identify 31 typical isolates on basis of their morphology, biochemical characteristics and production of metabolites. In addition, bacterial cells were hybridized with fluorescently labelled probes for Bacteroides/Prevotella and Clostridium genus. Four isolates were identified at the species level as Mitsuokella multiacidus, three isolates as Bacteroides capillosus and one isolate as Actinomyces izraeli. All isolates except the last one belong to the Bacteroidaceae family. One strain could be assigned to the Bacteroides/Prevotella genus on basis of the hybridization test. Other mucinolytic isolates were not identified as their characteristics did not correspond to any previously described bacterial species. No Clostridium sp. strain was detected. In two M. multiacidus strains high activities of extracellular mucin lyases were found. The pH-optimum of lyases was 6.2. Calcium cations were necessary for their optimal function. This work extends general knowledge about fermentation of carbohydrate and nitrogen substrates in rabbit caecum. Rabbit, caecum, mucin, bacteriaMucin is a glycoprotein present in the mucosal layer lining mammalian gastrointestinal, respiratory and reproductive tract. The carbohydrate moiety can be either an acidic mucopolysaccharide containing uronic acids and hexosamines or an oligosaccharide containing L-fucose and sialic acid (S alyers and Leedle 1983). Mucin composition is tissue specific and differs in different animal species. Mucin is a part of the defense mechanism as it prevents bacteria, viruses and dietary lectins from attaching to the intestinal or other epithelium. Another mucin function is the protection of the mucosal epithelium against acidic and proteolytic damage in the stomach and intestine. In the digestive tract, mucin insures a smooth passage of the foodpulp. Holmes et al. (1974) observed in pigs that large amounts of mucin were not digested in the small intestine, but fermented in the hindgut. Microorganisms responsible for mucin fermentation in the human colon are partially known. Salyers et al. (1977) isolated from the human colon several Bacteroides strains able to degrade mucins and plant polysaccharides. B ayliss and Houston (1984) identified some mucin fermenters as members of the Bacteroides genus, other resembled Bifidobacterium sp., Clostridium septicum, and Eubacterium sp. Crociani et al. (199...

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“…Several α-and β-L-arabinofuranoside degradative enzymes in B. longum might be involved in L-arabinose acquisition from plant polysaccharides and HRGPs in the large intestine. In fact, gum arabic containing type-II arabinogalactan and AGP are fermented by almost all strains of B. longum, but not by the other 28 species of bifidobacteria (11). B. longum, which is one of the predominant bifidobacterial species in the large intestine, is thought to contribute to maintaining the health of the large intestine by releasing acetate through metabolism of plant polysaccharides and HRGPs.…”

Section: G Effects Of Polysaccharides and Hrgps Containing L-arabinomentioning

confidence: 99%

“…In particular, 4 of the 7 gene clusters contained 9 candidate genes for α-L-arabinofuranosidase belonging to GH43 and 51. Several reports have indicated that B. longum has the ability to grow on various non-digestible plant carbohydrate polymers containing α-L-arabinofuranosyl linkages, e.g., arabinoxylan, arabinogalactan, and arabinan (11)(12)(13). The presence of degradative enzymes for plant carbohydrates may reflect the superior ability of B. longum to adapt to the intestinal environment.…”

Section: A Introductionmentioning

confidence: 99%

Functional Analysis of Degradative Enzymes for Hydroxyproline-linked ^|^beta;-L-Arabinofuranosides in Bifidobacterium longum

Fujita¹,

Kitahara²,

Suganuma³

2012

TIGG

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Abstractβ-L-Arabinofuranosides are hydroxyproline (Hyp)-linked sugar chains of extensin observed in plant cell wall fractions. Despite the broad distribution of β-Larabinofuranosyl residues in plants, degradative enzymes have not yet been identified. In 2011, we cloned and characterized the first degradative enzymes for Hyp-linked β-L-arabinofuranosides from Bifidobacterium longum. These enzymes were composed of a glycoside hydrolase (GH) family 43 α-L-arabinofuranosidase (HypAA) releasing L-arabinose from Arafα1-3Arafβ1-2Arafβ1-2Arafβ-Hyp, a GH121 β-L-arabinobiosidase (HypBA2) releasing Arafβ1-2Araf (β-Ara 2 ) from Arafβ1-2Arafβ1-2Arafβ-Hyp, and a GH127 β-L-arabinofuranosidase (HypBA1) degrading β-Ara 2 to L-arabinose. These enzymes are encoded in a conserved gene cluster on several B. longum genomes, but not in genome sequences of other intestinal bacteria. Hyp-linked β-L-arabinofuranosides were utilized as carbohydrate sources by B. longum. This review presents the functional features of enzymes for Hyp-linked β-L-arabinofuranosides and the predicted metabolic pathway in B. longum. A. IntroductionL-Arabinose residues are the main constituents of sugars in plant cell walls, and they are mostly present in the form of α-L-furanose in polysaccharides such as arabinan, arabinoxylan, and pectic arabinogalactan. Glycoside hydrolases involved in the degradation of α-Larabinofuranosides are present in 6 glycoside hydrolase (GH) families (GH3, GH43, GH51, GH54, GH62, and GH93) in the CAZy database. In addition, degradative enzymes for α-and β-L-arabinopyranoside linkages were also found in the GH42 and GH27 families, respectively (1,2). On the other hand, β-L-arabinofuranoside linkages constitute sugar chains of hydroxyproline-rich glycoproteins (HRGPs), which are known

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Degradation of complex carbohydrates by Bifidobacterium spp.

Cited by 137 publications

References 9 publications

Degradation of Guar Gum by Intestinal Bacteria

Degradation of Guar Gum by Intestinal Bacteria

Isolation, Identification and Characterization of Rabbit Caecal Mucinolytic Bacteria

Functional Analysis of Degradative Enzymes for Hydroxyproline-linked ^|^beta;-L-Arabinofuranosides in Bifidobacterium longum

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