Characterization of recombinant β- galactosidase and its use in enzymatic synthesis of lactulose from lactose and fructose

Liao, Xueyi; Zheng, Qianwang; Zhou, Qianling; Lin, Jizhen; Guo, Li‐Qiong; Fang, Yun

doi:10.1016/j.molcatb.2016.09.019

Cited by 14 publications

(2 citation statements)

References 43 publications

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“…The fructose was added in the ratio of 2:1 (lactose: fructose w:w). The E. coli-derived β-galactosidase was added at 1 U/mL, 2 U/mL, 3 U/mL, and 4 U/mL and reacted in a water bath at an optimum temperature of 50 • C and an optimum pH of 7 for 18 h [15]. HPLC was used to test the content of lactulose and lactose in the supernatants of the samples at 0 h, 3 h, 6 h, 12 h, and 18 h.…”

Section: Enzymatic Synthesis Of Lactulosementioning

confidence: 99%

Increase in Lactulose Content in a Hot-Alkaline-Based System through Fermentation with a Selected Lactic Acid Bacteria Strain Followed by the β-Galactosidase Catalysis Process

Guo,

Ma,

Song

et al. 2023

Foods

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In this study, lactic acid bacteria (LAB) fermentation and β-galactosidase catalysis methods were combined to increase the lactulose concentration and reduce the galactose and lactose content in a hot-alkaline-based system. The optimal conditions for chemical isomerization were 70 °C for 50 min for lactulose production, in which the concentration of lactulose was 31.3 ± 1.2%. Then, the selection and identification of LAB, which can utilize lactose and cannot affect lactulose content, were determined from 451 strains in the laboratory. It was found that Lactobacillus salivarius TM-2–8 had weak lactulose utilization and more robust lactose utilization. Lactobacillus rhamnosus grx.21 was weak in terms of lactulose utilization and strong in terms of galactose utilization. These two strains fermented the chemical isomerization system of lactulose to reduce the content of lactose and galactose. The results showed that the lactose concentration was 48.96 ± 2.92 g/L and the lactulose concentration was 59.73 ± 1. 8 g/L for fermentation lasting 18 h. The β-galactosidase was used to increase the content of lactulose in the fermented system at this time. The highest concentration of 74.89 ± 1.68 g/L lactulose was obtained at an enzymatic concentration of 3 U/mL and catalyzed at 50 °C for 3 h by β-galactosidase.

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Section: Enzymatic Synthesis Of Lactulosementioning

confidence: 99%

Increase in Lactulose Content in a Hot-Alkaline-Based System through Fermentation with a Selected Lactic Acid Bacteria Strain Followed by the β-Galactosidase Catalysis Process

Guo,

Ma,

Song

et al. 2023

Foods

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“…The efficient catalytic behavior and broad tolerance spectrum of enzyme against organic solvents, metal ions, high temperature and pH are responsible to broaden its utility profile at commercial level. The biochemical characterization of enzymes can boost up their catalytic efficiency over long period of time (Liu et al 2015;Liao et al 2016). Different microbial species are capable to release extracellular b-galactosidase but fungal strains are always preferred owing to the production of highly stable and catalytically efficient enzymes for industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Purification and catalytic behavior optimization of lactose degrading β-galactosidase from Aspergillus nidulans

et al. 2018

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The b-galactosidase is an industrially valuable enzyme and used to hydrolyze the lactose into glucose and galactose. Considering the broad utility profile in food industry, b-galactosidase from Aspergillus nidulans was purified and characterized in term of its catalytic properties and stability. It displayed highest catalytic efficiency at 60°C after 10.0 min within acidic pH environment (pH 5). The b-galactosidase exhibited 100% and 60% catalytic activity at 40°C and 50°C, respectively even after 120.0 min. The b-galactosidase activity was remained stable in the presence of Zn 2? , Ni 2? , and Mg 2? ions. The activity was also retained in all investigated organic solvents except DMSO at various ionic concentrations. The surfactants Triton X-100 and SDS caused positive impact on the catalytic activity of enzyme at 1.0 mM concentration. However, the percent relative activity of b-galactosidase was significantly reduced when incubated with EDTA. The molecular mass of b-galactosidase estimated to be 95 kDa. The SEM micrographs of ONPG before and after b-galactosidase treatment indicated a remarkable difference in the morphology and proved the strong catalytic strength of enzyme. The b-galactosidase also demonstrated exceptional storage stability at-80°C,-20°C and 4°C by retaining 86, 79 and 70% activity even after 100.0 days.

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Lactulose

Guerrero

Vera²,

Illanes³

2022

Handbook of Food Bioactive Ingredients

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Characterization of recombinant β- galactosidase and its use in enzymatic synthesis of lactulose from lactose and fructose

Cited by 14 publications

References 43 publications

Increase in Lactulose Content in a Hot-Alkaline-Based System through Fermentation with a Selected Lactic Acid Bacteria Strain Followed by the β-Galactosidase Catalysis Process

Increase in Lactulose Content in a Hot-Alkaline-Based System through Fermentation with a Selected Lactic Acid Bacteria Strain Followed by the β-Galactosidase Catalysis Process

Purification and catalytic behavior optimization of lactose degrading β-galactosidase from Aspergillus nidulans

Lactulose

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