Enzymatic synthesis of oligosaccharides

Monsan, P

doi:10.1016/0168-6445(94)00052-z

Cited by 17 publications

(30 citation statements)

References 18 publications

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“…The ability of coliforms to utilize prebiotic oligosaccharides has been contradictory. Several studies have reported that FOS can support growth of E. coli, Enterobacter and Salmonella (Wang and Gibson 1993;Hartemink et al 1997), while others have indicated no growth (Hidaka et al 1986;Mitsuoka et al 1987;Bailey et al 1991;Monsan and Paul 1995). VanLaere et al (2000) reported that arabinooligosaccharides could support growth of E. coli but FOS could not.…”

Section: Raffinose Productmentioning

confidence: 99%

“…Clostridium perfringens is a saccharolytic and pathogenic organism (Sneath 1986) that possesses a wide variety glycosidic enzymes and transporters for carbohydrate utilization (Shimizu et al 2002). It has been reported that C. perfringens cannot use FOS or GOS (Hidaka et al 1986;Monsan and Paul 1995). In contrast, VanLaere et al (2000) reported that a strain of C. perfringens fermented FOS.…”

Section: Raffinose Productmentioning

confidence: 99%

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Growth of various intestinal bacteria on alternansucrase-derived oligosaccharides

Holt

Miller-Fosmore

Côté

2005

Lett Appl Microbiol

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Aims: To determine whether alternansucrase (ASR)-derived oligosaccharides can support the in vitro growth of various intestinal bacteria. Methods and Results: Growth was assessed from each culture after incubation in a medium containing ASR-derived oligosaccharide as sole carbohydrate source. Most of the Bifidobacterium spp. tested showed growth on all five of the oligosaccharides tested while the Lactobacillus spp., Bacteroides thetaiotaomicron, coliforms and pathogenic bacteria displayed no or little growth. Conclusions: The ASR-derived oligosaccharides were selectively utilized by many of the Bifidobacterium spp. tested but did not support significant growth of the Lactobacillus spp., Bact. thetaiotaomicron, coliforms and pathogenic bacteria tested. Significance and Impact of the Study: Alternansucrase-derived oligosaccharides are a potential source of new prebiotics.

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Section: Raffinose Productmentioning

confidence: 99%

Section: Raffinose Productmentioning

confidence: 99%

Growth of various intestinal bacteria on alternansucrase-derived oligosaccharides

Holt

Miller-Fosmore

Côté

2005

Lett Appl Microbiol

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“…Glycosyltranferases (GTFs) are enzymes that catalyse the transfer of glycosyl residues from a donor molecule to a particular acceptor (Monsan and Paul 1995). Many bacteria produce significant amounts of EPSs.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of a glucosyltransferase and a rhamnosyltransferase fromStreptomycessp. 139

Wang

Bai

et al. 2010

Journal of Applied Microbiology

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Aims: Ste15 and ste22 present in the Ebosin biosynthesis gene cluster (ste) were previously shown to function in Ebosin biosynthesis and both of the protein products are predicted to be glycosyltransferases. In this study, their biochemical activities were confirmed. Methods and Results: ste15 and ste22 were cloned and expressed in Escherichia coli. With a continuous coupled spectrophotometric assay and using the purified proteins, we now demonstrated that the protein Ste15 has the ability of catalysing the transfer of glucose specifically from UDP‐glucose to an Ebosin precursor that lacks glucose, the lipid carrier located in the cytoplasmic membrane of the gene ste15 disrupt mutant Streptomyces sp. 139 (ste15−). The protein Ste22 can catalyse the transfer of rhamnose specifically from TDP‐rhamnose to an Ebosin precursor that lacks rhamnose, a lipophilic carrier in the cytoplasmic membrane of the gene ste22 disrupt mutant Streptomyces sp. 139 (ste22−). Conclusions: The gene product of ste15 was identified to be a glucosyltransferase, and the protein encoded by ste22 was found to be a rhamnosyltransferase. Significance and Impact of the Study: Both of two enzymes play essential roles in the formation of repeating units of sugars during Ebosin biosynthesis. These are the first glucosyltransferase and rhamnosyltransferase in the biosynthesis of a Streptomyces exopolysaccharide to be characterized.

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“…It is readily metabolized to short chain fatty acids by the colonic microbiota (Dills, 1989), being therefore considered as a potential prebiotic. It has been used also as a lactulose substitute in the treatment of hepatic encephalopathy and also as a low-calorie sweetener for diabetics (Monsan and Paul, 1995). Aside from the food sector, lactitol has been used as moisturizing agent, plasticizer and adhesive (Audic et al 2003).…”

Section: Products Derived From Lactosementioning

confidence: 99%

“…Prebiotic action is mostly assigned to GOS-3 and GOS-4 (Gopal et al 2001). Different from other lactose derived NDO, GOS are produced industrially by enzyme biocatalysis with microbial β-galactosidases (Gänzle et al 2008), chemical synthesis having been displaced for being more complex and environmentally objectionable (Monsan and Paul, 1995;Sears and Wong, 2001). The commercial products now available are rather impure preparations, with total GOS amounting about 50% of solids and significant variations, both in the kind of linkage and molecular size distribution, according to the origin of the enzyme used in their synthesis (Rastall, 2006;Crittenden and Playne, 2009 (Husain, 2010;Park and Oh, 2010).…”

Section: Enzymatic Synthesis Of Galacto-oligosacaccharides (Gos)mentioning

confidence: 99%

Whey upgrading by enzyme biocatalysis

Illanes¹

2011

Electro Journal of Biotech

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Whey is a co-product of processes for the production of cheese and casein that retains most of the lactose content in milk. World production of whey is estimated around 200 million tons per year with an increase rate of about 2%/per year. Milk production is seasonal, so surplus whey is unavoidable. Traditionally, whey producers have considered it as a nuisance and strategies of whey handling have been mostly oriented to their more convenient disposal. This vision has been steadily evolving because of the upgrading potential of whey major components (lactose and whey proteins), but also because of more stringent regulations of waste disposal. Only the big cheese manufacturing companies are in the position of implementing technologies for their recovery and upgrading, so there is a major challenge in incorporating medium and small size producers to a platform of whey utilization, conciliating industrial interest with environmental protection within the framework of sustainable development. Within this context, among the many technological options for whey upgrading, transformation of whey components by enzyme biocatalysis appears as prominent. In fact, enzymes are green catalysts that can perform a myriad of transformation reactions under mild conditions and with strict specificity, so reducing production costs and environmental burden. This review pretends to highlight the impact of biocatalysis within a platform of whey upgrading. Technological options are shortly reviewed and then an in-depth and critical appraisal of enzyme technologies for whey upgrading is presented, with a special focus on newly developed enzymatic processes of organic synthesis, where the added value is high, being then a powerful driving force for industrial implementation.

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Enzymatic synthesis of oligosaccharides

Cited by 17 publications

References 18 publications

Growth of various intestinal bacteria on alternansucrase-derived oligosaccharides

Growth of various intestinal bacteria on alternansucrase-derived oligosaccharides

Cloning and characterization of a glucosyltransferase and a rhamnosyltransferase fromStreptomycessp. 139

Whey upgrading by enzyme biocatalysis

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