A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c

Wanarska, Marta; Kur, Józef

doi:10.1186/1475-2859-11-113

Cited by 61 publications

(45 citation statements)

References 38 publications

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“…The equilibrium ratios of common aldoses and ketoses resulting from isomerases, however, are generally biased towards the ketoses, except for D-glucose/D-fructose 42) and Dgalactose/D-tagatose. 44) The equilibrium ratio of 6-deoxy-L-psicose to 6-deoxy-L-altrose was biased towards 6-deoxy-psicose in this study, although the ratio of 6-deoxy-L-altrose was greater than that of the common aldose L-altrose, which was generated from L-psicose (ratio 20:80, data not shown). These observations suggest that 6-deoxy-aldose is favored by isomerization, in contrast to the isomerization reactions between common aldoses and ketoses.…”

Section: )mentioning

confidence: 45%

Enzymatic production of three 6-deoxy-aldohexoses from l-rhamnose

Shompoosang

Yoshihara

Uechi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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6-Deoxy-l-glucose, 6-deoxy-l-altrose, and 6-deoxy-l-allose were produced from l-rhamnose with an immobilized enzyme that was partially purified (IE) and an immobilized Escherichia coli recombinant treated with toluene (TT). 6-Deoxy-l-psicose was produced from l-rhamnose by a combination of l-rhamnose isomerase (TT-PsLRhI) and d-tagatose 3-epimerase (TT-PcDTE). The purified 6-deoxy-l-psicose was isomerized to 6-deoxy-l-altrose and 6-deoxy-l-allose with l-arabinose isomerase (TT-EaLAI) and l-ribose isomerase (TT-AcLRI), respectively, and then was epimerized to l-rhamnulose with immobilized d-tagatose 3-epimerase (IE-PcDTE). Following purification, l-rhamnulose was converted to 6-deoxy-l-glucose with d-arabinose isomerase (TT-BpDAI). The equilibrium ratios of 6-deoxy-l-psicose:6-deoxy-l-altrose, 6-deoxy-l-psicose:6-deoxy-l-allose, and l-rhamnulose:6-deoxy-l-glucose were 60:40, 40:60, and 27:73, respectively. The production yields of 6-deoxy-l-glucose, 6-deoxy-l-altrose, and 6-deoxy-l-allose from l-rhamnose were 5.4, 14.6, and 25.1%, respectively. These results indicate that the aldose isomerases used in this study acted on 6-deoxy aldohexoses.

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Section: )mentioning

confidence: 45%

Enzymatic production of three 6-deoxy-aldohexoses from l-rhamnose

Shompoosang

Yoshihara

Uechi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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“…62 D-Tagatose, a natural rare monosaccharide, is an isomer of D-galactose which can be manufactured by the chemical or enzymatic isomerization of Dgalactose. 63,64 Among the biocatalysts, L-arabinose isomerase has been mostly applied for D-tagatose production because of the industrial feasibility for the use of D-galactose as a substrate. 64 D-Tagatose has attracted a great attention in recent years for its low caloric diet and can be used as sweetener in several foods, beverages, and dietary supplements.…”

Section: Isomerases (Ec5)mentioning

confidence: 99%

“…There are numerous reports indicates the useful medical properties of this sugar such as prebiotic, antioxidant and tooth-friendly as well as reduction of symptoms associated with type 2 diabetes, anemia, hemophilia and hyperglycemia. 63,65 L-arabinose isomerase from various bacteria have been identified and studied from a number of microbial sources, but little information is available about this enzyme from B. licheniformis, and L-arabinose isomerase specific towards only L-arabinose. 61 DNA sequence analysis of araA2 revealed an open reading frame of 1425 bp, capable of encoding a polypeptide of 474 amino acid residues with a calculated isoelectric point of pH 4.8 and a molecular mass of 53,500 Da.…”

Section: Isomerases (Ec5)mentioning

confidence: 99%

Identification and Molecular Characterization of Genes Coding Pharmaceutically Important Enzymes from Halo-Thermo Tolerant Bacillus

Safary¹,

Moniri²,

Hamzeh‐Mivehroud³

et al. 2016

Adv Pharm Bull

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“…A recombinant Pichia pastoris yeast strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus was constructed and a recombinant L-arabinose isomerase from psychrotolerant bacterium Arthrobacter sp. 22c was tried (Wanarska and Kur, 2012). The combination of the recombinant yeast strain and the enzyme in one reaction mixture containing whey permeate resulted in the simultaneous hydrolysis of lactose.…”

Section: Tagatosementioning

confidence: 99%

Other Organism‐Based Processes and Products

Lee

2014

Fundamentals of Food Biotechnology

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Enzymes, which are protein catalysts synthesized by living systems, are important as synthetic and degradative catalysts. With the help of a multitude of enzymes, microorganisms are able to carry out the huge number of stepwise chemical reactions necessary for the growth and maintenance of cells (metabolism). Many microorganisms synthesize additional, often complex substances, which play no part in the growth process, the so-called secondary metabolites such as flavor and fragrances. Most of the chemical reactions taking place in living cells are completed in milliseconds or less, within a relatively narrow range of physical conditions. This rapid rate of metabolism is due to the existence of biological catalysts, namely enzymes. Enzymes not only make essential contributions to cellular activities, but also find many applications in biotechnology, especially in the food processing industry, for manufacturing cheese, beer, wine, bread, sweeteners, and so on, and in the chemical and pharmaceutical industries for synthesizing amino acids and antibiotics.While the presence of natural enzymes is advantageous in curing food products such as cheese and meat to give desirable textures and flavors, natural enzymes may produce undesirable reactions, such as rancidity from lipases and browning reactions due to polyphenol oxidases. Sometimes natural enzymes in foods are used as an index of the pasteurization of milk or cheese (by the detection of phosphatase or catalase) or to indicate the presence of peroxidase in vegetable products (as evidence of incomplete blanching). Recognition of the functions and the usefulness of enzymes in bringing about desirable changes in foods has led to the large-scale production of commercial enzymes. Of the more than 4000 enzymes known from animal, plant, or microbial sources, fewer than 20 are industrially produced on a large scale for the production of foods and intermediates. The majority of enzymes are hydrolases such as amylases, cellulases, pectinases, and proteases, which degrade polymeric substances to simple molecules. The world market for total enzymes is predicted to $7 billion in 2013

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A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c

Cited by 61 publications

References 38 publications

Enzymatic production of three 6-deoxy-aldohexoses from l-rhamnose

Enzymatic production of three 6-deoxy-aldohexoses from l-rhamnose

Identification and Molecular Characterization of Genes Coding Pharmaceutically Important Enzymes from Halo-Thermo Tolerant Bacillus

Other Organism‐Based Processes and Products

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