Biochemical characterization of a novel β-galactosidase from Paenibacillus barengoltzii suitable for lactose hydrolysis and galactooligosaccharides synthesis

Liu, Yu; Zhou, C.; Jiang, Zhengqiang; Yan, Qiaojuan; Yang, Shaoqing

doi:10.1016/j.ijbiomac.2017.06.073

Cited by 43 publications

(42 citation statements)

References 44 publications

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“…However, when the concentration of borax is 40 mM, the complex of O4-O6 and O4-O3 with galactose is very weak [ 43 ], and at the same time, we found that no complex appeared in the measurement. In that pH range, the residual activity of Gal2A was similar to that of previously reported β-galactosidases ( Table 1 ), such as PbBGal2A from Paenibacillus barengoltzii [ 25 ], GalA from Alteromonas sp. ANT48 [ 23 ], and recombinant Gal from Alteromonas sp.…”

Section: Resultssupporting

confidence: 87%

“…Although various β-galactosidases have been cloned and identified, only a few of them can produce GOS by transglycosylation. Compared with other β-galactosidases that produce GOS, such as PbBGal2A from Paenibacillus barengoltzii [ 25 ] and GalA from Alteromonas sp. ANT48 [ 23 ], the TLC plates showed that Gal2A has the same high transglycosylation activity as these enzymes, which further demonstrated that Gal2A is a potential candidate for catalyzing the production of GOS.…”

Section: Resultsmentioning

confidence: 99%

“…Some organisms can produce β-galactosidases, including bacteria, fungi, and higher eukaryotes [ 23 ]. Usually, the β-galactosidases from eukaryotes mainly belong to GH35 [ 24 , 25 ], while bacteria-derived β-galactosidases are mainly in GH families 42 and 2 [ 25 , 26 , 27 , 28 ]. The microorganisms used for the commercial production of β-galactosidase mainly include Bifidobacterium longum , Bacillus subtilis , Lactobacillus , Aspergillus niger , and Kluyveromyces lactis [ 29 , 30 , 31 ].…”

Section: Introductionmentioning

confidence: 99%

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Cloning and Characterization of a New β-Galactosidase from Alteromonas sp. QD01 and Its Potential in Synthesis of Galacto-Oligosaccharides

et al. 2020

Marine Drugs

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As prebiotics, galacto-oligosaccharides (GOSs) can improve the intestinal flora and have important applications in medicine. β-galactosidases could promote the synthesis of GOSs in lactose and catalyze the hydrolysis of lactose. In this study, a new β-galactosidase gene (gal2A), which belongs to the glycoside hydrolase family 2, was cloned from marine bacterium Alteromonas sp. QD01 and expressed in Escherichia coli. The molecular weight of Gal2A was 117.07 kDa. The optimal pH and temperature of Gal2A were 8.0 and 40 °C, respectively. At the same time, Gal2A showed wide pH stability in the pH range of 6.0–9.5, which is suitable for lactose hydrolysis in milk. Most metal ions promoted the activity of Gal2A, especially Mn2+ and Mg2+. Importantly, Gal2A exhibited high transglycosylation activity, which can catalyze the formation of GOS from milk and lactose. These characteristics indicated that Gal2A may be ideal for producing GOSs and lactose-reducing dairy products.

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Section: Resultssupporting

confidence: 87%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cloning and Characterization of a New β-Galactosidase from Alteromonas sp. QD01 and Its Potential in Synthesis of Galacto-Oligosaccharides

et al. 2020

Marine Drugs

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“…The effects of D-glucose and D-galactose on the enzyme activity were estimated by determining the enzymatic activity in the presence of various concentration of these saccharides (5-250 mM D-glucose or D-galactose) at 40°C for 10 min in 50 mM phosphate buffer (pH 7.5) using 5 mM oNPG as the substrate [35]. Determination of the inhibition type (competitive or non-competitive) by these saccharides was conducted based on non-linear Lineweaver and Burk reciprocal plot.…”

Section: Effect Of Saccharides Metal Ions and Other Chemical Compoumentioning

confidence: 99%

Activation of LacZ gene in Escherichia coli DH5α via α-complementation mechanism for β-galactosidase production and its biochemical characterizations

Hamed

Khedr

Abdelraof

2020

Journal of Genetic Engineering and Biotechnology

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Background Plasmid propagation in recombination strains such as Escherichia coli DH5α is regarded as a beneficial instrument for stable amplification of the DNA materials. Here, we show trans-conjugation of pGEM-T cloning vector (modified Promega PCR product cloning vector with tra genes, transposable element (Tn5)) and M13 sequence via α-complementation mechanism in order to activate β-d-galactosidase gene in DH5α strain (non-lactose-fermenting host). Results Trans-conjugation with pGEM-T allows correction of LacZ gene deletion through Tn5, and successful trans-conjugants in DH5α host cells can be able to produce active enzyme, thus described as lactose fermenting strain. The intracellular β-galactosidase was subjected to precipitation by ammonium sulfate and subsequently gel filtration, and the purified enzyme showed a molecular weight of approximately 72-kDa sodium dodecyl sulfate-polyacrylamid gel electrophoresis. The purified enzyme activity showed an optimal pH and temperature of 7.5 and 40 °C, respectively; it had a high stability within pH 6–8.5 and moderate thermal stability up to 50 °C. Conclusion Trans-conjugant of E. coli DH5α- lacZ∆M15 was successfully implemented. UV mutagenesis of the potent trans-conjugant isolate provides an improvement of the enzyme productivity. The enzymatic competitive inhibition by d-galactose and hydrolysis of lactose at ambient temperatures could make this enzyme a promising candidate for use in the dairy industry.

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“…Novas β-galactosidases bem como tecnologias inovadoras ligadas à produção dessa enzima vêm sendo descobertas e estudadas pelos pesquisadores (DUAN et al, 2017;JOSE et al, 2017;LIU et al, 2017;YOU, Chang, et al, 2017;YOU, Zhang, et al, 2017). Erich et al (2015) realizaram uma triagem de 1,3 milhões de clones de metagenoma para descobrir novas β-galactosidases.…”

Section: Enzima β-Galactosidaseunclassified

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

Dantas¹,

Verruck²,

Prudêncio³

2019

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Biochemical characterization of a novel β-galactosidase from Paenibacillus barengoltzii suitable for lactose hydrolysis and galactooligosaccharides synthesis

Cited by 43 publications

References 44 publications

Cloning and Characterization of a New β-Galactosidase from Alteromonas sp. QD01 and Its Potential in Synthesis of Galacto-Oligosaccharides

Cloning and Characterization of a New β-Galactosidase from Alteromonas sp. QD01 and Its Potential in Synthesis of Galacto-Oligosaccharides

Activation of LacZ gene in Escherichia coli DH5α via α-complementation mechanism for β-galactosidase production and its biochemical characterizations

Ciência e Tecnologia de Leite e Produtos Lácteos Sem Lactose

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