The acid tolerant l-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive d-tagatose producer

Rhimi, Moez; Ilhammami, Rimeh; Bajic, Goran; Boudebbouze, Samira; Maguin, Emmanuelle; Haser, R.; Aghajari, Nushin

doi:10.1016/j.biortech.2010.07.036

Cited by 63 publications

(61 citation statements)

References 35 publications

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“…ANA-3 L -AI presented a relatively high specific activity of 164 U/mg making it more active than most L -AIs from mesophilic bacterial origin (Table 1). Only few of the currently characterized L -AIs exhibit higher specific activity, mainly those from thermophilic bacteria like B. stearothermophilus US100 (185 U/mg) and T. neapolitana (119 U/mg) or lactic acid bacteria as L. sakei (218 U/mg) [10,13,24]. …”

Section: Resultsmentioning

confidence: 99%

The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures

et al. 2011

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BackgroundL-arabinose isomerases catalyse the isomerization of L-arabinose into L-ribulose at insight biological systems. At industrial scale of this enzyme is used for the bioconversion of D-galactose into D-tagatose which has many applications in pharmaceutical and agro-food industries. The isomerization reaction is thermodynamically equilibrated, and therefore the bioconversion rates is shifted towards tagatose when the temperature is increased. Moreover, to prevent secondary reactions it will be of interest to operate at low pH. The profitability of this D-tagatose production process is mainly related to the use of lactose as cheaper raw material. In many dairy products it will be interesting to produce D-tagatose during storage. This requires an efficient L-arabinose isomerase acting at low temperature and pH values.ResultsThe gene encoding the L-arabinose isomerase from Shewanella sp. ANA-3 was cloned and overexpressed in Escherichia coli. The purified protein has a tetrameric arrangement composed by four identical 55 kDa subunits. The biochemical characterization of this enzyme showed that it was distinguishable by its maximal activity at low temperatures comprised between 15-35°C. Interestingly, this biocatalyst preserves more than 85% of its activity in a broad range of temperatures from 4.0 to 45°C. Shewanella sp. ANA-3 L-arabinose isomerase was also optimally active at pH 5.5-6.5 and maintained over 80% of its activity at large pH values from 4.0 to 8.5. Furthermore, this enzyme exhibited a weak requirement for metallic ions for its activity evaluated at 0.6 mM Mn2+. Stability studies showed that this protein is highly stable mainly at low temperature and pH values. Remarkably, T268K mutation clearly enhances the enzyme stability at low pH values. Use of this L-arabinose isomerase for D-tagatose production allows the achievement of attractive bioconversion rates of 16% at 4°C and 34% at 35°C.ConclusionsHere we reported the purification and the biochemical characterization of the novel Shewanella sp. ANA-3 L-arabinose isomerase. Determination of the biochemical properties demonstrated that this enzyme was highly active at low temperatures. The generated T268K mutant displays an increase of the enzyme stability essentially at low pH. These features seem to be very attractive for the bioconversion of D-galactose into D-tagatose at low temperature which is very interesting from industrial point of view.

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Section: Resultsmentioning

confidence: 99%

The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures

et al. 2011

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“…In contrast, very little activity could be detected on the mirror image substrates L-lyxose and L-mannose [54]. Many more isomerases have been shown to be active on sugars similar to their wild-type substrates [2,12,57,71,85,86,88,94,117].…”

Section: Isomerasesmentioning

confidence: 85%

“…L-Arabinose isomerase for tagatose production L-Arabinose isomerase (L-AI) has been thoroughly studied for the conversion of D-galactose into the low-calorie sweetener D-tagatose [9,10,14,89,94]. Tagatose is almost as sweet as sucrose but is metabolized in a different fashion, resulting in a caloric content that is about threefold lower [19,60].…”

Section: Isomerasesmentioning

confidence: 99%

Enzymes for the biocatalytic production of rare sugars

Beerens

Desmet

Soetaert

2012

Journal of Industrial Microbiology and Biotechnology

165

109

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Carbohydrates are much more than just a source of energy as they also mediate a variety of recognition processes that are central to human health. As such, saccharides can be applied in the food and pharmaceutical industries to stimulate our immune system (e.g., prebiotics), to control diabetes (e.g., low-calorie sweeteners), or as building blocks for anticancer and antiviral drugs (e.g., L: -nucleosides). Unfortunately, only a small number of all possible monosaccharides are found in nature in sufficient amounts to allow their commercial exploitation. Consequently, so-called rare sugars have to be produced by (bio)chemical processes starting from cheap and widely available substrates. Three enzyme classes that can be used for rare sugar production are keto-aldol isomerases, epimerases, and oxidoreductases. In this review, the recent developments in rare sugar production with these biocatalysts are discussed.

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“…However, the thermostability and conversion ratio results of BTAI indicate that BTAI is more stable than the L-AI of L. sakei at above 40 C and has a relatively high conversion ratio as compared to L. sakeiderived L-AI. 10) Overall, the features of BTAI suggest that it is a good candidate for potential application in D-tagatose production in the food and pharmaceutical industries. …”

Section: )mentioning

confidence: 99%

Characterization of an L-Arabinose Isomerase from Bacillus thermoglucosidasius for D-Tagatose Production

Seo

2013

Bioscience, Biotechnology, and Biochemistry

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The acid tolerant l-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive d-tagatose producer

Cited by 63 publications

References 35 publications

The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures

The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures

Enzymes for the biocatalytic production of rare sugars

Characterization of an <small>L</small>-Arabinose Isomerase from <i>Bacillus thermoglucosidasius</i> for <small>D</small>-Tagatose Production

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