Toxicological studies on Lactose Oxidase from Microdochium nivale expressed in Fusarium venenatum

Ahmad, Sharique; Brinch, D.S.; Friis, Esben P.; Pedersen, P.B.

doi:10.1016/j.yrtph.2004.02.003

Cited by 26 publications

(19 citation statements)

References 22 publications

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“…Proteins searched for and analysed in cultures of P. taetrolens were exocrine enzymeslactose oxidase with molecular mass of 55 kDa [6]and lactonase with molecular mass of 28 kDa [10]…”

Section: Electrophoretic Analysis Of Proteins In Cultures Of Pseudomomentioning

confidence: 99%

“…The enzyme used in this study was produced by a submerged fermentation of Fusarium venenatum and contained a gene code from Microdochium nivale [6]. …”

Section: Introductionmentioning

confidence: 99%

“…One of the new applications in focus is converting lactose in milk to lactobionic acid and exploiting the desirable characteristics of lactobionic acid to replace proteins and/or fats in process, cheeses and cream cheese. Lactobionic acid may even be seen as a flavour enhancer, a texture builder, and antioxidant synergist [6]. …”

Section: Introductionmentioning

confidence: 99%

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The Utilization of Pseudomonas taetrolens to Produce Lactobionic Acid

Goderska

Szwengiel

Czarnecki

2014

Appl Biochem Biotechnol

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Lactobionic acid is a relatively new product derived from lactose oxidation, with high potential applications as a bioactive compound. Conducted experiments confirmed that both the time and temperature influenced the production of lactobionic acid during bioconversion of lactose using the Pseudomonas taetrolens bacteria. The study also investigated the effect of inoculum concentration on the production of lactobionic acid as a result of oxidation of whey-derived lactose. The highest concentration of lactobionic acid during oxidation of whey-derived lactose at a temperature of 30 °C by microorganisms. P. taetrolens was obtained during 50-h oxidation of the medium, which contained 25 % addition of the inoculum, in which the count of live cells was 2.85 × 109 CFU/ml.

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“…Proteins searched for and analysed in cultures of P. taetrolens were exocrine enzymeslactose oxidase with molecular mass of 55 kDa [6]and lactonase with molecular mass of 28 kDa [10]…”

Section: Electrophoretic Analysis Of Proteins In Cultures Of Pseudomomentioning

confidence: 99%

“…The enzyme used in this study was produced by a submerged fermentation of Fusarium venenatum and contained a gene code from Microdochium nivale [6]. …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Utilization of Pseudomonas taetrolens to Produce Lactobionic Acid

Goderska

Szwengiel

Czarnecki

2014

Appl Biochem Biotechnol

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“…It is able to oxidize several mono-, oligo-, and polymeric saccharides and transfer their electrons to molecular oxygen-thus producing hydrogen peroxide which can be removed by the addition of catalase-or to other electron acceptors. It has been shown that the enzyme can be considered as safe for use in the food industry (Ahmad et al, 2004).…”

mentioning

confidence: 99%

Oxidation of lactose to lactobionic acid by a Microdochium nivale carbohydrate oxidase: Kinetics and operational stability

Nordkvist

Nielsen

2007

Biotech & Bioengineering

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Oxidation of lactose to lactobionic acid by a Microdochium nivale carbohydrate oxidase was studied. The K(m)-value for lactose, obtained by a traditional enzymatic assay, was 0.066 mM at pH 6.4 and 38 degrees C. The effect of oxygen on the enzymatic rate of reaction as well as the operational stability of the enzyme was studied by performing reactions at constant pH and temperature in a stirred tank reactor. Catalase was included in all reactions to avoid inhibition and deactivation of the oxidase by hydrogen peroxide. At pH 6.4 and 38 degrees C, K(m) for oxygen was 0.97 mM, while the catalytical rate constant, k(cat), was 94 s(-1). Furthermore, we found that the operational stability of the oxidase was dependent on the type of base used for neutralization of the acid produced. Thus, when 2 M NaOH was used for neutralization of a reaction medium containing 50 mM phosphate buffer, significant deactivation of the oxidase was observed. Also, we found that the oxidase was protected against deactivation by base at high lactose concentrations. A simple model is proposed to explain the obtained results.

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“…The mechanism of the C1 oxidation by oxygen is a Ping Pong mechanism (Kulys et al, 2001). This oxidase can be considered as safe for use in human food (Ahmad, Brinch, Friis, & Pedersen, 2004). COXMn can also be used in biosensors for glucose determination in blood (Kulys, Tetianec, & Schneider, 2000), in the catalysis of the biotransformation of lactose into the value-added product lactobionic acid (Nordkvist, Nielsen, & Villadsen, 2007), in the generation of bleaching agents in liquid detergents (Pricelius, Ludwig, Lant, Haltrich, & Guebitz, 2011) and as a dough or bread improver (Arnaut, De Meyer, & Van Haesendonck, 2006;Christensen et al, 1999;Oestergaard & De Maria, 2011).…”

Section: Introductionmentioning

confidence: 99%