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

@article{Synowiecki2006SourcesPA,
  title={Sources, Properties and Suitability of New Thermostable Enzymes in Food Processing},
  author={J. Synowiecki and B. Grzybowska and A. Zdziebło},
  journal={Critical Reviews in Food Science and Nutrition},
  year={2006},
  volume={46},
  pages={197 - 205}
}
Investigations concerning recombinant α-amylases from Pyrococcus woesei and thermostable α-glucosidase from Thermus thermophilus indicate their suitability for starch processing. Furthermore, the study of recombinant β-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… Expand
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References

SHOWING 1-10 OF 86 REFERENCES
New source of the thermostable α-glucosidase suitable for single step starch processing
Abstract Thermus thermophilus contains α-glucosidase that is located in the cell cytoplasm. The highest enzyme activity was achieved after 25–30 h of microorganism cultivation at 70 °C in a mediumExpand
Isolation and some properties of β-galactosidase from the thermophilic bacterium Thermus thermophilus
Abstract The highest β -galactosidase activity in Thermus thermophilus cells was achieved after 40 h of cultivation at 70°C in a medium containing 0.8% peptone, 0.4% yeast extract and 0.2% NaCl.Expand
Isolation and some properties of the thermostable β-galactosidase of Pyrococcus woesei expressed in Escherichia coli
TLDR
The enzyme with β-galactosidase activity from E. coli BL21 (DE3) transformant containing the gene encoding enzyme from Pyrococcus woesei was isolated using cell extraction and the increase in the enzyme specific activity was determined using ONPG as substrate. Expand
Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei
The cultivation of the hyperthermophilic archaeobacterium Pyrococcus woesei on starch under continuous gassing (80% H2:20% CO2) caused the formation of 250 U/l of an extremely thermoactive andExpand
Cloning of the thermostable α-amylase gene from Pyrococcus woesei in Escherichia coli
TLDR
The thermostable α-amylase can be purified free of most of the bacterial protein and released from fusion with intein by heat treatment at about 75°C in the presence of thiol compounds, and shows remarkable activity toward glycogen but not toward pullulan. Expand
Hydrolysis of lactose by beta-glycosidase CelB from hyperthermophilic archaeon Pyrococcus furiosus: comparison of hollow-fiber membrane and packed-bed immobilized enzyme reactors for continuous processing of ultrahigh temperature-treated skim milk.
TLDR
Recombinant beta-glycosidase CelB from the hyperthermophilic archaeon Pyrococcusfuriosus was produced through expression of the plasmid-encoded gene in Escherichia coli and its performance during continuous processing of ultrahigh temperature-treated skim milk at 70 degrees C was analyzed regarding long-term stability, productivity, and diffusional limitation thereof. Expand
Hydrolysis of Lactose by ß-Glycosidase CelB from Hyperthermophilic Archaeon Pyrococcus Furiosus
Recombinant s-glycosidase CelB from the hyperthermophilic archaeon Pyrococcus furiosus was produced through expression of the plasmid-encoded gene in Escherichia coli. Bioreactor cultivations of E.Expand
Purification and characterization of a Bacillus sp. SAM1606 thermostable α-glucosidase with transglucosylation activity
TLDR
High thermostability of the enzyme permits the transglucosylation reaction at high temperatures, which would be beneficial for continuous production of oligosaccharides from sucrose. Expand
Hydrolysis of lactose by free and immobilized beta-galactosidase from Thermus sp. strain T2.
TLDR
The immobilization reduced the activity of the enzyme, but increased its thermal stability, and a comparison between the kinetic behavior of this thermophilic enzyme and enzymes of mesophile microorganisms previously studied by us and by other authors is performed. Expand
Thermostable β-galactosidase from the archaebacterium Sulfolobus solfataricus Purification and properties
A thermophilic and thermostable P-galactosidase activity was purified to homogeneity from crude extracts of the archaebacterium Suljiulobus sovuturicus, by a procedure including ion-exchange andExpand
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