2005
DOI: 10.1016/j.procbio.2005.05.007
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Facile synthesis of glucose-1-phosphate from starch by Thermus caldophilus GK24 α-glucan phosphorylase

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Cited by 14 publications
(14 citation statements)
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“…Glycoside phosphorylases, in contrast, only need inorganic phosphate to produce a glycosylphosphate. In literature, the synthesis of α-glucose-1-phosphate (αGlc1P) from starch [10,11] or sucrose [12] and that of α-galactose-1-phosphate (αGal1P) from lactose [13,14] have previously been reported. A production process for βGlc1P has not yet been described in detail, but is similarly feasible using GH65 disaccharide phosphorylases from cheap substrates [15] briefly mention the production of βGlc1P from trehalose, using typical reaction conditions employed for αGlc1P [16].…”
Section: Introductionmentioning
confidence: 99%
“…Glycoside phosphorylases, in contrast, only need inorganic phosphate to produce a glycosylphosphate. In literature, the synthesis of α-glucose-1-phosphate (αGlc1P) from starch [10,11] or sucrose [12] and that of α-galactose-1-phosphate (αGal1P) from lactose [13,14] have previously been reported. A production process for βGlc1P has not yet been described in detail, but is similarly feasible using GH65 disaccharide phosphorylases from cheap substrates [15] briefly mention the production of βGlc1P from trehalose, using typical reaction conditions employed for αGlc1P [16].…”
Section: Introductionmentioning
confidence: 99%
“…It has been observed that most known phosphorylases have a subunit molecular mass of around 90 kDa and usually exist as homodimers or tetramers (Palm et al 1985). At 25°C the thermostable α-glucan phosphorylases from Thermus thermophilus, Thermus caldophilus and Thermococcus litoralis form octamers, hexamers and trimers, respectively (Boeck and Schinzel 1996, Xavier et al 1999, Bae et al 2005.…”
Section: Cloning and Purification Of The Pf1535 Proteinmentioning
confidence: 99%
“…Significant progress has been made with the detailed structural and functional characterization of glycogen phosphorylases of mesophilic origins (Chen and Segel 1968, Hwang and Fletterick 1986, Browner et al 1991, Rogers et al 1992, Srivastava et al 1996; however, little is known about those from hyperthermophilic organisms. Thermostable α-glucan phosphorylases reported to date have been isolated from the thermophilic bacteria Bacillus stearothermophilus, Thermus caldophilus, Thermus aquaticus, Thermus thermophilus, Thermotoga maritima and Aquifex aeolicus (Konig et al 1982, Boeck and Schinzel 1996, Bibel et al 1998, Takata et al 1998, Takaha et al 2001, Bhuiyan et al 2003, Bae et al 2005. Among archaea, the enzyme activity has been detected in Methanococcus maripaludis and Thermococcus litoralis (Yu et al 1994, Xavier et al 1999.…”
Section: Introductionmentioning
confidence: 99%
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“…In the case of recombinant E. coli MP, a removal of trace phosphatase amounts cleaving Glc1P was essential and this could be achieved neither by aYnity precipitation with starch, or precipitation with Bioprocessing Agent BAP 1050 (Toso Haas, Stuttgart, Germany), nor by ion-exchange chromatography (Q-Sepharose, Pharmacia) or anion-exchange membrane Wltration (CIDE 1000, CIQM 1000, Millipore) [3]. Later, thermostable MPs from Thermus caldophilus [4,5] and Thermoanaerobacter tengcongensis [6] were explored for Glc1P production. In addition to the obvious potential advantage of higher process temperature to promote better solubilization and disorganization of the raw materials [7], thermostable enzymes can be overexpressed in a mesophilic host whose enzymes are completely inactivated during the thermal reaction.…”
Section: Introductionmentioning
confidence: 99%