Maltodextrin Phosphorylase from <i>Escherichia coli</i>: Production and Application for the Synthesis of α‐Glucose‐1‐Phosphatea

Nidetzky, Bernd; Weinhäusel, Andreas; Haltrich, Dietmar; Kulbe, Klaus D.; Schinzel, Reinhard

doi:10.1111/j.1749-6632.1996.tb40562.x

Cited by 7 publications

(2 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This often prevents one-pot synthesis in the presence of two phosphorylases and requires that α-D-glucose 1-phosphate is prepared first in a separate reaction. Synthesis of β-D-glucose 1-phosphate from maltose [68,76] and trehalose [77] also lacks efficiency; however, because of its relevance as glucosyl donor for both enzymatic and chemical glucosylation reactions, the concept of a coupled one-pot phosphorolysis/reverse phosphorolysis reaction using maltose phosphorylase was examined. The costly intermediary β-D-glucose 1-phosphate, obtained from maltose in the presence of only a twofold excess of phosphate, is directly used as substrate for reverse phosphorolysis with different monosaccharides, resulting in >84% yield of new α-(1→ 4)-glucosidic disaccharides [78].…”

Section: Multi-step Enzymatic Synthesis Of Disaccharides and Other Glmentioning

confidence: 99%

Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences

Luley‐Goedl

Nidetzky

2010

Biotechnology Journal

Self Cite

View full text Add to dashboard Cite

Disaccharide phosphorylases are glycosyltransferases (EC 2.4.1.α) of specialized carbohydrate metabolism in microorganisms. They catalyze glycosyl transfer to phosphate using a disaccharide as donor substrate. Phosphorylases for the conversion of naturally abundant disaccharides including sucrose, maltose, α,α‐trehalose, cellobiose, chitobiose, and laminaribiose have been described. Structurally, these disaccharide phosphorylases are often closely related to glycoside hydrolases and transglycosidases. Mechanistically, they are categorized according the stereochemical course of the reaction catalyzed, whereby the anomeric configuration of the disaccharide donor substrate may be retained or inverted in the sugar 1‐phosphate product. Glycosyl transfer with inversion is thought to occur through a single displacement‐like catalytic mechanism, exemplified by the reaction coordinate of cellobiose/chitobiose phosphorylase. Reaction via configurational retention takes place through the double displacement‐like mechanism employed by sucrose phosphorylase. Retaining α,α‐trehalose phosphorylase (from fungi) utilizes a different catalytic strategy, perhaps best described by a direct displacement mechanism, to achieve stereochemical control in an overall retentive transformation. Disaccharide phosphorylases have recently attracted renewed interest as catalysts for synthesis of glycosides to be applied as food additives and cosmetic ingredients. Relevant examples are lacto‐N‐biose and glucosylglycerol whose enzymatic production was achieved on multikilogram scale. Protein engineering of phosphorylases is currently pursued in different laboratories with the aim of broadening the donor and acceptor substrate specificities of naturally existing enzyme forms, to eventually generate a toolbox of new catalysts for glycoside synthesis.

show abstract

Section: Multi-step Enzymatic Synthesis Of Disaccharides and Other Glmentioning

confidence: 99%

Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences

Luley‐Goedl

Nidetzky

2010

Biotechnology Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…G1P is usually produced by enzyme-mediated biocatalysis but not produced by microbial fermentation because high polarity of sugar phosphates prevents them from crossing intact cell membrane . It can be produced from numerous oligosaccharides catalyzed by their respective glycoside phosphorylases, e.g., sucrose and sucrose phosphorylase, cellobiose and cellobiose phosphorylase, cellodextrin and cellodextrin phosphorylase, and maltodextrin , or soluble starch, along with αGP. However, previous methods of G1P production have shown several weaknesses.…”

Section: Introductionmentioning

confidence: 99%

One-Pot Biosynthesis of High-Concentration α-Glucose 1-Phosphate from Starch by Sequential Addition of Three Hyperthermophilic Enzymes

Zhou

You²,

et al. 2016

J. Agric. Food Chem.

View full text Add to dashboard Cite

α-Glucose 1-phosphate (G1P) is synthesized from 5% (w/v) corn starch and 1 M phosphate mediated by α-glucan phosphorylase (αGP) from the thermophilic bacterium Thermotoga maritima at pH 7.2 and 70 °C. To increase G1P yield from corn starch containing branched amylopectin, a hyper-thermostable isoamylase from Sulfolobus tokodaii was added for simultaneous starch gelatinization and starch-debranching hydrolysis at 85 °C and pH 5.5 before αGP use. The pretreatment of isoamylase increased G1P titer from 120 mM to 170 mM. To increase maltose and maltotriose utilization, the third thermostable enzyme, 4-glucanotransferase (4GT) from Thermococcus litoralis, was added during the late stage of G1P biotransformation, further increasing G1P titer to 200 mM. This titer is the highest G1P level obtained on starch or its derived products (maltodextrin and soluble starch). This study suggests that in vitro multienzyme biotransformation has an advantage of great engineering flexibility in terms of space and time compared with microbial fermentation.

show abstract

Fusion of a family 9 cellulose-binding module improves catalytic potential of Clostridium thermocellum cellodextrin phosphorylase on insoluble cellulose

Zhu

Zhang

et al. 2011

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Clostridium thermocellum cellodextrin phosphorylase (CtCDP), a single-module protein without an apparent carbohydrate-binding module, has reported activities on soluble cellodextrin with a degree of polymerization (DP) from two to five. In this study, CtCDP was first discovered to have weak activities on weakly water-soluble celloheptaose and insoluble regenerated amorphous cellulose (RAC). To enhance its activity on solid cellulosic materials, four cellulose binding modules, e.g., CBM3 (type A) from C. thermocellum CbhA, CBM4-2 (type B) from Rhodothermus marinus Xyn10A, CBM6 (type B) from Cellvibrio mixtus Cel5B, and CBM9-2 (type C) from Thermotoga maritima Xyn10A, were fused to the C terminus of CtCDP. Fusion of any selected CBM with CtCDP did not influence its kinetic parameters on cellobiose but affected the binding and catalytic properties on celloheptaose and RAC differently. Among them, addition of CBM9 to CtCDP resulted in a 2.7-fold increase of catalytic efficiency for degrading celloheptaose. CtCDP-CBM9 exhibited enhanced specific activities over 20% on the short-chain RAC (DP = 14) and more than 50% on the long-chain RAC (DP = 164). The chimeric protein CtCDP-CBM9 would be the first step to construct a cellulose phosphorylase for in vitro hydrogen production from cellulose by synthetic pathway biotransformation (SyPaB).

show abstract

Maltodextrin Phosphorylase from Escherichia coli: Production and Application for the Synthesis of α‐Glucose‐1‐Phosphatea

Cited by 7 publications

References 24 publications

Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences

Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences

One-Pot Biosynthesis of High-Concentration α-Glucose 1-Phosphate from Starch by Sequential Addition of Three Hyperthermophilic Enzymes

Fusion of a family 9 cellulose-binding module improves catalytic potential of Clostridium thermocellum cellodextrin phosphorylase on insoluble cellulose

Contact Info

Product

Resources

About