Improving Properties of a Novel β-Galactosidase from Lactobacillus plantarum by Covalent Immobilization

Benavente, R.; Pessela, Benevides C.; Curiel, José Antonio; Rivas, Blanca de las; Múñoz, Rosario; Guisán, José M.; Mancheño, José M.; Cardelle‐Cobas, Alejandra; Ruiz‐Matute, Ana I.; Corzo, Nieves

doi:10.3390/molecules20057874

Cited by 22 publications

(9 citation statements)

References 27 publications

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“…Besides the use of commercial enzymatic preparations, the synthesis of β‐GOSLu was also reported for β‐galactosidases obtained from crude cell extracts of Kluyveromyces strains isolated from artisanal cheese (Padilla and others ) and α‐galactosidase from Lactobacillus plantarum overexpressed in E. coli (Benavente and others ). The use of β‐galactosidase from L. plantarum involved its prior immobilization via multipoint covalent attachment on glyoxyl–agarose, which significantly increased its stability.…”

Section: Lactulose As a Substrate Of Other Enzymatic Reactionsmentioning

confidence: 99%

“…The use of β‐galactosidase from L. plantarum involved its prior immobilization via multipoint covalent attachment on glyoxyl–agarose, which significantly increased its stability. The carbohydrate mixture obtained at pH 5.0, 45 °C, 450 g/L lactulose, and 1 g of derivative containing 5 U/mL, was composed of monosaccharides, β‐(1→6)‐galactobiose, lactulose, 6′galactosyl‐lactulose (8.5 g/100 g of total carbohydrate), 1‐galactosyl‐lactulose (9.5 g/100 g of total carbohydrate), a new trisaccharide identified as 3′galactosyl‐lactulose (9 g/100 g of total carbohydrate), and other unidentified β‐GOSLu (5 g/100 g of total carbohydrate) (Benavente and others ). On the other hand, the synthesis of β‐GOSLu by α‐galactosidases from crude cell extracts of K. lactis and K marxianus , under the conditions described by Martínez‐Villaluenga and others (), led to the identification of only 2 trisaccharides, 6′galactosyl‐lactulose, 1‐galactosyl‐lactulose (Padilla and others ).…”

Section: Lactulose As a Substrate Of Other Enzymatic Reactionsmentioning

confidence: 99%

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Biocatalytic Approaches Using Lactulose: End Product Compared with Substrate

Silvério

Macedo

Teixeira

et al. 2016

Comp Rev Food Sci Food Safe

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Lactulose is a lactose-based carbohydrate with well-known prebiotic effect and recognized medical applications. Currently, the commercially available lactulose is chemically synthesized. Nevertheless, the process leads to low yields and high levels of by-products. Alternatively, lactulose can be produced by enzymatic synthesis, which provides a cleaner production under mild conditions. Two different enzymatic routes were reported for lactulose production. Lactulose can be obtained through hydrolysis and transfer reactions catalyzed by a glycosidase. Alternatively, lactulose can be produced by direct isomerization of lactose to lactulose catalyzed by cellobiose-2-epimerase. An interesting characteristic of lactulose is also its capacity to act as substrate in additional enzymatic synthesis which leads to the formation of attractive compounds, such as lactulose-based oligosaccharides and lactulose esters. Besides increasing the interest and potential of lactulose, these lactulose-based compounds can also offer new and promising functionalities and applications. Herein, we review the enzymes involved in the synthesis of lactulose, as well as the reaction conditions and yields. The potential of different enzymes is discussed and it is shown that reaction conditions and composition of products depend on the type of enzyme and its microbial source. The conversion of lactulose into lactulose-based compounds is also covered, describing in detail the biocatalysts involved, the reaction conditions used, and the potential of the final products obtained.

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Section: Lactulose As a Substrate Of Other Enzymatic Reactionsmentioning

confidence: 99%

Section: Lactulose As a Substrate Of Other Enzymatic Reactionsmentioning

confidence: 99%

Biocatalytic Approaches Using Lactulose: End Product Compared with Substrate

Silvério

Macedo

Teixeira

et al. 2016

Comp Rev Food Sci Food Safe

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“…However, the cost of β-galactosidase and its sensitivity to environmental changes have limited its utilisation [ 2 ]. Immobilisation techniques have been shown to enable easier separation of enzymes from reaction media to facilitate enzyme reuse, while also enhancing enzyme performance by improving enzyme stability, activity, specificity, and selectivity and reducing inhibition [ 3 , 4 , 5 , 6 , 7 ]. For instance, the stabilisation of monomeric enzymes can be improved by multipoint covalent attachment or generation of favourable environments surrounding enzymes [ 8 ], while the stabilisation of multimeric enzymes can be boosted by multi-subunit covalent immobilisation to avoid subunit dissociation [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes

et al. 2017

Molecules

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β-galactosidase was successfully encapsulated within an amino-functionalised silica matrix using a “fish-in-net” approach and molecular imprinting technique followed by covalent binding of lysozyme via a glutaraldehyde-based method. Transmission electron microscopy (TEM), X-ray diffraction (XRD), scanning electron microscopy (SEM), and Fourier transform infrared (FTIR) spectroscopy were used to characterise the silica matrix hosting the two enzymes. Both encapsulated β-galactosidase and bound lysozyme exhibited high enzymatic activities and outstanding operational stability in model reactions. Moreover, enzyme activities of the co-immobilised enzymes did not obviously change relative to enzymes immobilised separately. In antibacterial tests, bound lysozyme exhibited 95.5% and 89.6% growth inhibition of Staphylococcus aureus ATCC (American type culture collection) 653 and Escherichia coli ATCC 1122, respectively. In milk treated with co-immobilised enzymes, favourable results were obtained regarding reduction of cell viability and high lactose hydrolysis rate. In addition, when both co-immobilised enzymes were employed to treat milk, high operational and storage stabilities were observed. The results demonstrate that the use of co-immobilised enzymes holds promise as an industrial strategy for producing low lactose milk to benefit people with lactose intolerance.

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“…The whey is produced by the processing and manufacturing of raw milk into products such as yogurt, ice cream, butter, and cheese through processes such as pasteurization, coagulation, filtration, centrifugation, chilling, etc. [11].…”

Section: Galactosidasesmentioning

confidence: 99%

Microbial Glycosidases for Nondigestible Oligosaccharides Production

Bezerra¹,

Montibra

Hansen

et al. 2017

Enzyme Inhibitors and Activators

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There is much interest in the study and production of nondigestible oligosaccharides (NDOs), due to their bioactivities and beneficial effects to the human health. The main approach in the production of NDOs relies on the action of glycosidases performing hydrolysis or transglycosylation of polysaccharides and sugars. In this chapter, a description of the main microbial glycosidases used for NDOs production, their sources, their principal properties, and a description of the production processes with the better results obtained are discussed.

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Improving Properties of a Novel β-Galactosidase from Lactobacillus plantarum by Covalent Immobilization

Cited by 22 publications

References 27 publications

Biocatalytic Approaches Using Lactulose: End Product Compared with Substrate

Biocatalytic Approaches Using Lactulose: End Product Compared with Substrate

Prevention of Bacterial Contamination of a Silica Matrix Containing Entrapped β-Galactosidase through the Action of Covalently Bound Lysozymes

Microbial Glycosidases for Nondigestible Oligosaccharides Production

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