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

  title={Sources, Properties and Suitability of New Thermostable Enzymes in Food Processing},
  author={J{\'o}zef Synowiecki and Beata Grzybowska and Anna Zdziebło},
  journal={Critical Reviews in Food Science and Nutrition},
  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… 
Improvement of functional properties of a thermostable β‐glycosidase for milk lactose hydrolysis
The immobilization process had a big impact on the catalysis performance, leading to an enhancement of the enzymatic reaction rate on lactose, as demonstrated by the increasing of 2 and 2.5 folds of Kcat and Kcat/KM, respectively.
Production, purification, and characterization of a potential thermostable galactosidase for milk lactose hydrolysis from Bacillus stearothermophilus.
The results suggest that this recombinant thermostable enzyme may be suitable for both the hydrolysis of lactose and the production of galactooligosaccharides in milk processing.
Preparation of lactose-free pasteurized milk with a recombinant thermostable β-glucosidase from Pyrococcus furiosus
The thermostablity of this recombinant β-glucosidase, combined with its neutral pH activity and favorable temperature activity optima, suggest that this enzyme is an ideal candidate for the hydrolysis of lactose in milk, and it would be suitable for application in low-lactose milk production during pasteurization.
Expression and characterization of α-Amylases from penicillium citrinum with bread as growth substrate
In an attempt to enhance the industrial production of α-amylases in the tropics, sterile fresh bread was inoculated with spore suspensions of Penicillium citrinum at 25 o C. Extracellular α-amylases
Immobilization of α-Amylase from Anoxybacillus sp. SK3-4 on ReliZyme and Immobead Supports
To the best of the authors' knowledge, this is the first report of an immobilization study of an α-amylase from Anoxybacillus spp.
Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification
A gene encoding amylopullulanase (gt-apu) of the extremely thermophilic Geobacillus thermoleovorans NP33 was cloned and expressed in Escherichia coli and the end-product analysis confirmed that this is an endoacting enzyme.
Chlorogenic Acid Oxidation by a Crude Peroxidase Preparation: Biocatalytic Characteristics and Oxidation Products
This study aimed at investigating the use of a crude peroxidase (POD) preparation from onion solid by-products for oxidizing chlorogenic acid (CGA), a widespread phenolic acid, various derivatives of which may occur in foods and food wastes.
Improving the catalytic activity of hyperthermophilic Pyrococcus prolidases for detoxification of organophosphorus nerve agents over a broad range of temperatures
To obtain a better enzyme for OP nerve agent decontamination and to investigate structural factors that influence protein thermostability and thermoactivity, randomly mutated P. furiosus prolidase mutants with improved activity over a broader range of temperatures were isolated.
Halophilic alkali- and thermostable amylase from a novel polyextremophilic Amphibacillus sp. NM-Ra2.
  • N. Mesbah, J. Wiegel
  • Chemistry, Medicine
    International journal of biological macromolecules
  • 2014


Isolation and some properties of the thermostable β-galactosidase of Pyrococcus woesei expressed in Escherichia coli
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.
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 caused the formation of 250 U/l of an extremely thermoactive and thermostable α-amylase, which hydrolyzed exclusively α-1,4-glycosidic linkages present in glucose polymers of various sizes.
Cloning of the thermostable α-amylase gene from Pyrococcus woesei in Escherichia coli
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.
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.
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.
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 and seems to reflect mainly binding of the soluble enzyme to the membrane surface of the hollow-fiber module.
Purification and characterization of a Bacillus sp. SAM1606 thermostable α-glucosidase with transglucosylation activity
High thermostability of the enzyme permits the transglucosylation reaction at high temperatures, which would be beneficial for continuous production of oligosaccharides from sucrose.
Hydrolysis of lactose by free and immobilized beta-galactosidase from Thermus sp. strain T2.
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.
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 and