Co-expression of l-arabinose isomerase and d-glucose isomerase in E. coli and development of an efficient process producing simultaneously d-tagatose and d-fructose

Rhimi, Moez; Messaoud, Ezzedine Ben; Borgi, Mohamed Ali; khadra, Khalifa Ben; Béjar, Samír

doi:10.1016/j.enzmictec.2006.10.032

Cited by 44 publications

(33 citation statements)

References 17 publications

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“…This strain belongs to the lactic acid bacteria which are considered by FAO and WHO as GRAS organisms. Consequently, it can be directly employed in industrial bioprocesses for production of value-added products from cheese whey or other industrial by-products (Rhimi et al, 2007). Finally, current studies are centered on non-recombinant L-arabinose isomerase production, purification and characterization from chosen wild-type strains.…”

Section: Discussionmentioning

confidence: 99%

Screening and selection of wild strains for L-arabinose isomerase production

Manzo

Simonetta

Rubiolo

et al. 2013

Braz. J. Chem. Eng.

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-The majority of L-arabinose isomerases have been isolated by recombinant techniques, but this methodology implies a reduced technological application. For this reason, 29 bacterial strains, some of them previously characterized as L-arabinose isomerase producers, were assayed as L-arabinose fermenting strains by employing conveniently designed culture media with 0.5% (w/v) L-arabinose as main carbon source. From all evaluated bacterial strains, Enterococcus faecium DBFIQ ID: E36, Enterococcus faecium DBFIQ ID: ETW4 and Pediococcus acidilactici ATCC ID: 8042 were, in this order, the best L-arabinose fermenting strains. Afterwards, to assay L-arabinose metabolization and L-arabinose isomerase activity, cell-free extract and saline precipitated cell-free extract of the three bacterial cultures were obtained and the production of ketoses was determined by the cysteine carbazole sulfuric acid method. Results showed that the greater the L-arabinose metabolization ability, the higher the enzymatic activity achieved, so Enterococcus faecium DBFIQ ID: E36 was selected to continue with production, purification and characterization studies. This work thus describes a simple microbiological method for the selection of L-arabinose fermenting bacteria for the potential production of the enzyme L-arabinose isomerase.

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Section: Discussionmentioning

confidence: 99%

Screening and selection of wild strains for L-arabinose isomerase production

Manzo

Simonetta

Rubiolo

et al. 2013

Braz. J. Chem. Eng.

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“…On the other hand, the analysis of operational stability showed that L-AI d-fructose chitosan derivative kept the activity above 80 % after 10 recirculation cycles at 60 °C whereas Rhimi et al [44] reported activity results above 70 % after 8 cycles with Bacillus stearothermophilus US100 L-AI entrapped in 6 % (w/v) of sodium alginate on BaCl 2 beads. Furthermore, Oh et al [27] used particles produced with 4 % (w/v) sodium alginate and treated with 0.2 (v/v) glutaraldehyde, which gave good results for 8 days (or cycles), although the activity of the biocatalyst rapidly decreased.…”

Section: L-arabinose Isomerase Immobilized On Comercial Resinsmentioning

confidence: 95%

“…Several researches have reported the use of different organic matrixes-such as sodium alginate [26,27,32,44,65], mesoporous aminopropyl glass [64], polyethylenimine [24], agarose [29] and CNBr-agarose for L-AI immobilization and production of d-tagatose [43]. However, these researches have not gone much deeper into the understanding of the enzyme immobilization process or have explored the possibilities of chitosan for the achievement of stable enzyme biocatalysts.…”

Section: L-arabinose Isomerase Immobilized On Comercial Resinsmentioning

confidence: 99%

Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach

Manzo

Sousa

Fenoglio

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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D-tagatose is produced from D-galactose by the enzyme L-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, D-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit(®) C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) D-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U g (gel) (-1) with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U g (gel) (-1) with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.

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“…GI obtained from different sources such as Flavobacterium , Bacillus , and some Streptomyces and Arthrobacter species is immobilized on different support materials such as DEAE cellulose (Chen and Anderson 1979 ;Huitron and Limon-Lason 1978 ), polyacrylamide gel (Demirel et al 2006 ;Strandberg and Smiley 1971 ), and alginate beads (Rhimi et al 2007 ).…”

Section: High-fructose Syrupmentioning

confidence: 99%

Industrial Enzyme Applications in Biorefineries for Starchy Materials

Gohel¹,

Dong

Maisuria³

2013

Advances in Enzyme Biotechnology

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This chapter reviews recent advances in technology developments in biorefi nery industries through enzymatic approaches where various starchy materials have been used as feedstock for biofuel and various syrup productions. It further discusses the enzymes discovery, industrial challenges, and how enzymatic-based approaches help different industries to develop environmentally sustainable and cost-effective solutions by making industrial process into more simplifi ed without compromising the product and by-product yields and their qualities.

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Co-expression of l-arabinose isomerase and d-glucose isomerase in E. coli and development of an efficient process producing simultaneously d-tagatose and d-fructose

Cited by 44 publications

References 17 publications

Screening and selection of wild strains for L-arabinose isomerase production

Screening and selection of wild strains for L-arabinose isomerase production

Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach

Industrial Enzyme Applications in Biorefineries for Starchy Materials

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