Challenges and perspectives of the β-galactosidase enzyme

Damin, Brenda Isadora Soares; Kovalski, F C; Fischer, Janaína; Piccin, Jeferson Steffanello; Dettmer, Aline

doi:10.1007/s00253-021-11423-7

Cited by 29 publications

(15 citation statements)

References 112 publications

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“…To date, a number of microbial β-galactosidases have been reported to catalyze transglycosylation of galactose to lactose, while the majority of them belong to GH2 family. 1,2,7 A large number of β-galactosidases from GH42 family, such as β-galactosidase from E. acetylicum 38 and K. oxytoca ZJUH1705, 17 had shown a low transgalactosylation activity, which was in agreement with the results of the present study.…”

Section: Analysis Of Hydrolytic Products and Transgalactosylation Pro...supporting

confidence: 92%

“…β‐Galactosidases (EC. 3.2.1.23) are exo‐glycosidases that cleavage the glycosidic linkage between the nonreducing terminal β‐ d ‐galactosyl residues and the aglycone moiety 1,2 . As an important class of enzymes, β‐galactosidases are widely distributed in nature, including microorganisms, plants, and animals.…”

Section: Introductionmentioning

confidence: 99%

“…3.2.1.23) are exo-glycosidases that cleavage the glycosidic linkage between the nonreducing terminal β-d-galactosyl residues and the aglycone moiety. 1,2 As an important class of enzymes, βgalactosidases are widely distributed in nature, including microorganisms, plants, and animals. Among them, microbial β-galactosidases have noticeably attracted scholars' attention due to their high activities, high yields, and abundance.…”

Section: Introductionmentioning

confidence: 99%

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A GH42 β‐galactosidase from Bifidobacterium thermophilum: Biochemical characterization and synthesis of galactosyl glycerol by reverse hydrolysis

Duan

Jia

Cao

et al. 2022

Biotech and App Biochem

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In this study, a β‐galactosidase gene (btgal42) was first cloned from Bifidobacterium thermophilum and successfully expressed in Escherichia coli. The molecular weight of the purified BtGal42 was estimated to be 78 kDa by the sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and 225 kDa by the size‐exclusion chromatography, indicating that the native BtGal42 was a homotrimer. BtGal42 belonged to the glycosidase hydrolase family 42, exhibiting the maximum activity at pH of 7 and at temperature of 50°C. The enzyme displayed a strictly specific activity toward substrates with β‐galactosyl linkages at the nonreducing ends, of which the activity on 4‐nitrophenyl‐β‐d‐galactopyranoside was the highest, followed by 2‐nitrophenyl‐β‐d‐galactopyranoside and lactose. Among the tested metals and reagents, BtGal42 showed tolerance in the presence of various organic solvents. Importantly, BtGal42 exhibited a high reverse hydrolysis activity when using galactose as the donor and the di‐alcohol ethylene glycol and the trialcohol glycerol as the acceptors. Under unoptimized reaction conditions, the galactosyl glycerol yield reached 62.2 g/L (galactose conversion rate, 41.2%). This study might provide a feasible method for the biosynthesis of galactosyl glycerol from low‐cost glycerol and galactose, which was associated with high conversion efficiency and few byproducts.

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Section: Analysis Of Hydrolytic Products and Transgalactosylation Pro...supporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A GH42 β‐galactosidase from Bifidobacterium thermophilum: Biochemical characterization and synthesis of galactosyl glycerol by reverse hydrolysis

Duan

Jia

Cao

et al. 2022

Biotech and App Biochem

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“…The counterpoint of this type of method is the decrease in enzymatic activity. It can occur due to some possible damage caused to the structural conformation of the enzyme [103] or the connection between the support and the amino acid residues in the active site.…”

Section: Core‐shell Polymeric Particles For Enzyme Immobilizationmentioning

confidence: 99%

A Comprehensive Review on Core‐Shell Polymeric Particles for Enzyme Immobilization

et al. 2022

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The search for ideal solid support that promotes enzyme stability, easy separation and reuse cycles in different processes has grown widely. In this sense, core‐shell polymer particles draw attention because they are already widely used in adsorption, catalysis, and drug delivery, due to their remarkable advantages in surface properties adjustment, excellent mechanical stability, and high chemical resistance, as a result of the combination of the characteristics of the polymers that form the core and shell of the structure. Thus, this review article provides an overview of the synthesis processes of these particles, highlighting the characteristics that can be obtained from each synthesis technique, as well as the most recently used techniques to obtain polymeric particles with core‐shell morphology. The advantages and main challenges for the application of these structures in the immobilization of enzymes are also discussed, providing a general summary of what has been explored in the literature. Despite the potential of application, the use of these materials in the immobilization of enzymes is still little explored, with studies focused mainly on lipases and around the same classes of polymers. Therefore, there is an opportunity window regarding the investigation of the immobilization of other enzymes of commercial interest on these polymeric supports.

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“…β-Galactosidase (β-gal) is an essential enzyme in plants, animals and microorganisms and it catalyzes the hydrolysis of β-galactoside into galactose and glucose. 1 In humans, β-gal activity correlates with cellular senescence that can lead to various diseases. 2 The β-gal assay, which tracks the enzyme activity of β-gal using an artificial chromogenic substrate, is routinely performed in genetics and in molecular biology.…”

mentioning

confidence: 99%