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

Li, Dandan; Li, Shangyong; Wu, Yuan; Jin, Man-Wen; Zhou, Yu; Wang, Yanan; Chen, Xuehong; Han, Yantao

doi:10.3390/md18060312

Cited by 19 publications

(31 citation statements)

References 43 publications

(57 reference statements)

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“…Optimisation regarding temperature were observed by previously (Hsu et al, 2005, Gobinath et al, 2014, Li et al, 2020 where β-gal synthesis was stable at 40 to 45°C, however, 35°C was found to be optimum for L. fermentum and above 50°C there was a rapid decrease in enzyme synthesis as well for the growth of the organism due to thermostability of enzyme (Cho et al, 2003;Rao and Dutta, 1977). β-gal production was prominent in the range 5.5 to 7.0 (p<0.05) as reported by others (Gobinath and Prapulla, 2014).…”

Section: Discussionmentioning

confidence: 71%

Optimal Production of β-Galactosidase from Lactobacillus fermentum for the Synthesis of Prebiotic Galactooligosaccharides (Gos)

Mahadevaiah¹,

Basavaiah²,

Parida³

et al. 2020

J Pure Appl Microbiol

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The enzyme β-galactosidase (β-gal) has extensively used for improvement of lactose intolerance condition. Present study, was designed to assess the potential of β-gal enzyme produced by Lactobacillus fermentum, a kefir isolate, as a biocatalyst for the manufacture of prebiotic galactooligosaccharides (GOS) from lactose. The efficiency of L. fermentum to produce β-gal of 4,254 u/ml was determined by permeabilizing the cells with solvents such as sodium dodecyl sulfate (SDS) and chloroform. Different parameters contributing β-gal production including reaction time, temperature, pH, carbohydrates, and substrate concentration on L. fermentum were studied and optimum β-gal activity was found to be 6,232.13 u/ml. It was observed that different experimental parameters for pH (7.0), temperature (35°C), and carbohydrates (galactose) were statistically significant (p<0.05). L. fermentum was found to produce GOS by transgalactosylation catalysed by β-gal during lactose hydrolysis which yielded di, tri, and tetra oligosaccharides, confirmed by TLC and HPLC. The culture showed β-gal activity, suggesting biotechnological applications and a promising organism for industrial β-gal production.

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Section: Discussionmentioning

confidence: 71%

Optimal Production of β-Galactosidase from Lactobacillus fermentum for the Synthesis of Prebiotic Galactooligosaccharides (Gos)

Mahadevaiah¹,

Basavaiah²,

Parida³

et al. 2020

J Pure Appl Microbiol

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“…Therefore, we expressed it in the baculovirus expression system, and high enzyme activity was detected. The optimal pH and temperature for β‐galactosidase of many bacteria and fungi were found in the range of 6.5–4.5 and 40–60 °C, respectively (Carneiro, Yu, Dupree, & Ward, 2018; Li et al, 2020; Xia et al, 2018; Yang et al, 2018). However, the optimum pH and temperature of some β‐galactosidase are not in this range, for example, β‐galactosidase from Aspergillus lacticoffeatus (Cardoso, Silverio, Abrunhosa, Teixeira, & Rodrigues, 2017).…”

Section: Discussionmentioning

confidence: 99%

“…Most metal ions promoted the activity of β‐galactosidase from Alteromonas sp . QD01, especially Mn 2+ and Mg 2+ (Li et al, 2020). According to the analysis of influences caused by metal ions to BmGal, we found that iron ions can stimulate the activity of the enzyme while cobalt, nickel, or lead ions can inhibit its activity significantly.…”

Section: Discussionmentioning

confidence: 99%

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Cloning, expression, and characteristic analysis of the novel β‐galactosidase from silkworm, Bombyx mori

Yao

Zong

et al. 2021

Genesis

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β-galactosidase is a critical exoglycosidase involved in the hydrolysis of lactose, the modi cation and degradation of glycoprotein in vivo. In this study, the β-galactosidase gene of silkworm (BmGal), whose cDNA comprises 11 exons and contains an intact ORF of 1821bp, was cloned. The protein sequence of BmGal showed high similarity with other known insect β-galactosidases. No activity of the BmGal expressed in Escherichia coli or Pichia pastoris was detected while it was successfully expressed with high enzyme activity in baculovirus-silkworm expression system, and the electrophoresis result revealed that the BmGal showed activity in oligomer mode. Enzyme activity assay showed that its optimum pH was 8.4 and its optimum temperature was 40℃. What's more, we found that iron ions can stimulate the activity of the enzyme while cobalt, nickel or lead ions can inhibit its activity signi cantly. Besides, the temporal-spatial expression pattern of the BmGal mRNA level was analyzed, which showed that BmGal was expressed at the highest level in the fth larval instar but relatively low level in the pupal and adult stage, and the highest expression level of BmGal was found in testis among all the tissues concerned.

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“…β-Galactosidase (EC 3.2.1.23), also referred to as lactase, is an important member of glycosyl hydrolase, which can hydrolyze O -glycosidic bonds of lactose by hydrolysis reaction, resulting in the production of glucose and galactose ( Vera et al, 2017 ; Singh et al, 2019 ). Treating dairy products with β-galactosidase through pre-hydrolyzation that can reduce lactose concentration offers a promising solution ( Li et al, 2020 ). Thus far, numerous β-galactosidases were purified, cloned, and characterized from bacteria ( Mavromatis et al, 2010 ; Tian et al, 2013 ), fungi ( Rico-Díaz et al, 2017 ), yeast ( de Freitas et al, 2020 ), plants ( Deng et al, 2019 ), and mammals ( He et al, 2008 ).…”

Section: Introductionmentioning

confidence: 99%

Characterization and Application of a New β-Galactosidase Gal42 From Marine Bacterium Bacillus sp. BY02

Zhou

Han

et al. 2021

Front. Microbiol.

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β-Galactosidase plays an important role in medicine and dairy industry. In this study, a new glycoside hydrolase family 42 (GH42) β-galactosidase-encoding gene, gal42, was cloned from a newly isolated marine bacterium Bacillus sp. BY02 and expressed in Escherichia coli. Structural characterization indicated that the encoding β-galactosidase, Gal42, is a homotrimer in solution, and homology modeling indicated that it retains the zinc binding sites of the Cys cluster. The reaction activity of Gal42 was significantly increased by Zn2+ (229.6%) and other divalent metal ions (Mn2+, Mg2+, and Co2+), while its activity was inhibited by EDTA (53.9%). Meanwhile, the thermo-stability of the Gal42 was also significantly enhanced by 5 and 10 mM of zinc ion supplement, which suggested that the “Cys-Zn” motif played important roles in both structural stability and catalytic function. Furthermore, Gal42 showed effective lactose hydrolysis activity, which makes the enzyme hydrolyze the lactose in milk effectively. These properties make Gal42 a potential candidate in food technology.

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

Cited by 19 publications

References 43 publications

Optimal Production of β-Galactosidase from Lactobacillus fermentum for the Synthesis of Prebiotic Galactooligosaccharides (Gos)

Optimal Production of β-Galactosidase from Lactobacillus fermentum for the Synthesis of Prebiotic Galactooligosaccharides (Gos)

Cloning, expression, and characteristic analysis of the novel β‐galactosidase from silkworm, Bombyx mori

Characterization and Application of a New β-Galactosidase Gal42 From Marine Bacterium Bacillus sp. BY02

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