Kinetic modeling of a bi‐enzymatic system for efficient conversion of lactose to lactobionic acid

Hecke, Wouter Van; Bhagwat, Aditya; Ludwig, Roland; Dewulf, Jo; Haltrich, Dietmar; Langenhove, Herman Van

doi:10.1002/bit.22165

Cited by 46 publications

(31 citation statements)

References 21 publications

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“…One was the application of a bubble-less membrane contactor, which greatly reduced enzyme inactivation, [102] together with a careful optimisation of the CDH/redox mediator/laccase ratio. [103] The other focussed on the continuous electrochemical regeneration of ABTS, thus avoiding air bubbles. A carbon felt anode (4.34 cm 2 , 0.106 g), a platinum wire cathode and a Ag j AgCl reference electrode were placed in an electrolysis cell (25 mL) and sodium acetate buffer of pH 5.5, lactose, ABTS and T. versicolor CDH were added.…”

Section: Bioelectrosynthesismentioning

confidence: 99%

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

et al. 2010

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Cellobiose dehydrogenase catalyses the oxidation of aldoses--a simple reaction, a boring enzyme? No, neither for the envisaged bioelectrochemical applications nor mechanistically. The catalytic cycle of this flavocytochrome is complex and modulated by its flexible cytochrome domain, which acts as a built-in redox mediator. This intramolecular electron transfer is modulated by the pH, an adaptation to the environmental conditions encountered or created by the enzyme-producing fungi. The cytochrome domain forms the base from which electrons can jump to large terminal electron acceptors, such as redox proteins, and also enables by that path direct electron transfer from the catalytically active flavodehydrogenase domain to electrode surfaces. The application of electrochemical techniques to the elucidation of the molecular and catalytic properties of cellobiose dehydrogenase is discussed and compared to biochemical methods. The results lead to valuable insights into the function of this cellulose-bound enzyme, but also form the basis of exciting applications in biosensors, biofuel cells and bioelectrocatalysis.

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Section: Bioelectrosynthesismentioning

confidence: 99%

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

et al. 2010

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“…The productivity of this study is as efficient as some previous studies (Van Hecke et al . ,b, ). However, the productivity is still lower comparisons with some others previous studies.…”

Section: Resultsmentioning

confidence: 99%

“…Although lactose is not a native electron donor for CDH, CDH efficiently oxidizes lactose at the C‐1 position of the reducing sugar moiety to lactobionolactone which spontaneously hydrolyses to lactobionic acid (Van Hecke et al . ). Lactobionic acid is a high value‐added lactose derivative.…”

Section: Introductionmentioning

confidence: 97%

Production of lactobionic acid from lactose using the cellobiose dehydrogenase-3-HAA-laccase system fromPycnoporussp. SYBC-L10

Tian

Yan

Huang

et al. 2018

Lett Appl Microbiol

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The aim of this study was to produce lactobionic acid from lactose by a new Pycnoporus sp. SYBC-L10 strain. Recently, studies on enzymatic production of lactobionic acid mostly focus on cellobiose dehydrogenase from Sclerotium rolfsii CBS 191·62 and laccase from Trametes pubescens MB 89 oxidize lactose to lactobionic acid with redox mediators. In this study, we converted lactose to lactobionic acid by shaking flask fermentation without exogenous mediator in the reaction mixture. In this bioconversion process, lactose is efficiently converted into lactobionic acid with a specific productivity of up to 3·1 g l h and 96% yield. 3-Hydroxyanthranilic acid added externally to the reaction mixture can obviously accelerate the conversion of lactose to lactobionic acid. The results showed that 3-hydroxyanthranilic acid produced by the fungus itself is an important influencing factor in this bioconversion process. This study presents the first attempt to efficiently produce lactobionic acid by white-rot fungi, suggesting definite potential for Pycnoporus to produce lactobionic acid. SIGNIFICANCE AND IMPACT OF THE STUDY: Lactobionic acid has been applied to a wide range of applications in pharmaceutical, food, nanotechnology and chemical industries. Here, an attempt was done to produce lactobionic acid from lactose using the cellobiose dehydrogenase-3-HAA-laccase system in a fermentation system. After a survey of other methods to produce lactobionic acid by cellobiose dehydrogenase, this study explores a new and significant perspective for the production of lactobionic acid.

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“…Lactobionic acid (4-O-β-galactopyranosyl-D-gluconato) is produced industrially by chemical oxidation of lactose ) even though the enzymatic synthesis has been reported with glucose-fructose oxidoreductase (Satory et al 1997) and also with cellobiose dehydrogenase in a dual enzymatic-electrochemical process (Dhariwal et al 2006) and in a fully enzymatic process with cellobiose dehydrogenase and laccase for electron replenishment (van Hecke et al 2009). It is a powerful chelating agent used in calcium supplement tablets, as sequestrant in detergents and also in organ preservation for transplants (Gänzle et al 2008).…”

Section: Products Derived From Lactosementioning

confidence: 97%

Whey upgrading by enzyme biocatalysis

Illanes¹

2011

Electro Journal of Biotech

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Whey is a co-product of processes for the production of cheese and casein that retains most of the lactose content in milk. World production of whey is estimated around 200 million tons per year with an increase rate of about 2%/per year. Milk production is seasonal, so surplus whey is unavoidable. Traditionally, whey producers have considered it as a nuisance and strategies of whey handling have been mostly oriented to their more convenient disposal. This vision has been steadily evolving because of the upgrading potential of whey major components (lactose and whey proteins), but also because of more stringent regulations of waste disposal. Only the big cheese manufacturing companies are in the position of implementing technologies for their recovery and upgrading, so there is a major challenge in incorporating medium and small size producers to a platform of whey utilization, conciliating industrial interest with environmental protection within the framework of sustainable development. Within this context, among the many technological options for whey upgrading, transformation of whey components by enzyme biocatalysis appears as prominent. In fact, enzymes are green catalysts that can perform a myriad of transformation reactions under mild conditions and with strict specificity, so reducing production costs and environmental burden. This review pretends to highlight the impact of biocatalysis within a platform of whey upgrading. Technological options are shortly reviewed and then an in-depth and critical appraisal of enzyme technologies for whey upgrading is presented, with a special focus on newly developed enzymatic processes of organic synthesis, where the added value is high, being then a powerful driving force for industrial implementation.

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Kinetic modeling of a bi‐enzymatic system for efficient conversion of lactose to lactobionic acid

Cited by 46 publications

References 21 publications

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications

Production of lactobionic acid from lactose using the cellobiose dehydrogenase-3-HAA-laccase system fromPycnoporussp. SYBC-L10

Whey upgrading by enzyme biocatalysis

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