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Ulezlo, I. V.; Tsereteli, A. K.; Portnaya, Irina; Am, Bezborodov

doi:10.1023/a:1002888207704

Cited by 2 publications

(4 citation statements)

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“…Our studies confirmed data reported previously, on the role of various ions on the activity of GIs from other microorganisms [1,3,[27][28][29]. We demonstrated, however, that the effects of Co 2+ and Mg 2+ on the rate of monosaccharide isomerization are less pronounced in the case of non-growing cells of A. nicotianae .…”

Section: Methodssupporting

confidence: 92%

“…The reaction of D -glucose to D -fructose isomerization was initially studied in cell-free extracts of Pseudomonas hydrophyla (1955-57) [1]. The enzyme glucose isomerase (GI; xylose ketol-isomerase, EC 5.3.1.5) has thus far been detected in more than 100 species of microorganisms [1].…”

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confidence: 99%

“…The enzyme glucose isomerase (GI; xylose ketol-isomerase, EC 5.3.1.5) has thus far been detected in more than 100 species of microorganisms [1]. The enzymatically active substance exhibiting GI activity is one of the several large-capacity enzyme preparations (together with amylases and proteases).…”

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confidence: 99%

“…A wide front of works on isolation and characterization of GI, preparation of heterogeneous biocatalysts for glucose isomerization, and development of domestic technologies for GFS manufacturing had been carried out in the USSR (as well as worldwide) during the 1980s [1,[5][6][7][8][9]. However, the crisis of the 1990s precluded the industrial introduction of these technologies.…”

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confidence: 99%

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10.1007/s10438-008-2008-9

2000

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Kinetics of monosaccharide isomerization has been studied in suspensions of intact, non-growing Arthrobacter nicotianae cells. Under the conditions of the study, glucose and fructose were isomerized at the same maximum rate of 700 µ mol/min per 1 g dried cells, which increased with temperature (the dependence was linear at 60-80 ° C). The proposed means of adsorption immobilization of A. nicotianae cells involve inorganic carriers differing in macrostructure, chemical nature, and surface characteristics. Biocatalysts obtained by adsorbing the cells of A. nicotianae on carbon-containing foamed ceramics in the coarse of submerged cultivation were relatively stable and retained original activity (catalysis of monosaccharide isomerization) throughout 14 h of use at 70 ° C. Maximum glucose isomerase activity (2 µ mol/min per 1 g) was observed with biocatalysts prepared by adsorption of non-growing A. nicotianae cells to the macroporous carbon-mineral carrier Sapropel and subsequent drying of the cell suspension together with the carrier.

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Section: Methodssupporting

confidence: 92%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Sources, Properties and Suitability of New Thermostable Enzymes in Food Processing

Synowiecki

Grzybowska

Zdziebło

2006

Critical Reviews in Food Science and Nutrition

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Investigations concerning recombinant a-amylases from Pyrococcus woesei and thermostable a-glucosidase from Thermus thermophilus indicate their suitability for starch processing. Furthermore, the study of recombinant ss-galactosidase from Pyrococcus woesei suitable for purpose of low lactose milk and whey production are also presented. The activity of this enzyme in a wide pH range of 4.3-6.6 and high thermostability suggests that it can be used for processing of dairy products at temperatures which restrict microbial growth during a long operating time of continuous-flow reactor with an immobilized enzyme system. Preparation of recombinant a-amylase and ss-galactosidase was facilitated by cloning and expression of genes from Pyrococcus woesei in Escherichia coli host. Satisfactory level of recombinant enzymes purification was achieved by thermal precipitation of native proteins originated from Escherichia coli. The obtained a-amylase has maximal activity at pH 5.6 and 93 degrees C. The half-life of this preparation (pH 5.6) at 90 degrees C and 110 degrees C was 11 h and 3.5 h, respectively, and retained 24% of residual activity following incubation for 2 h at 120 degrees C. An advantageous attribute of recombinant a -amylase is independence of its activity and stability on calcium salt. a-Glucosidase from Thermus thermophilus also not require metal ions for stability and retained about 80% of maximal activity at pH range 5.8-6.9. Thus, this enzyme can be used together with recombinant a-amylase.

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Cited by 2 publications

References 10 publications

10.1007/s10438-008-2008-9

10.1007/s10438-008-2008-9

Sources, Properties and Suitability of New Thermostable Enzymes in Food Processing

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