Beta‐galactosidase technology: A solution to the lactose problem

Shukla, Triveni Piasad; Wierzbicki, L.E.

doi:10.1080/10408397509527178

Cited by 124 publications

(55 citation statements)

References 80 publications

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“…Bacteria, yeast and fungi are all good sources of p-galactosidase: however there are important differences between the 362 G. MOULIN AND P. GALZY p-galactosidases from different sources. Their main features have been reviewed by Shukla (1975) The hydrolysis can be carried out with solu ble enzymes (Nipjels, 1978;Nipjels and Rheinlander, 1982;Giacin et aI., 1974): in this case the enzyme preparation is lost with each production batch. This process has often been llsed for the lactose hydrolysis of milk.…”

Section: Hydrolysis Oj'lactose \-Vuh Catalytic Resin Chemical Hydrolmentioning

confidence: 99%

Whey, a Potential Substrate for Biotechnology

Moulin¹,

Galzy²

1984

Biotechnology and Genetic Engineering Reviews

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Section: Hydrolysis Oj'lactose \-Vuh Catalytic Resin Chemical Hydrolmentioning

confidence: 99%

Whey, a Potential Substrate for Biotechnology

Moulin¹,

Galzy²

1984

Biotechnology and Genetic Engineering Reviews

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“…[5,6] Commercialized b-galactosidase mainly derives from Escherichia coli, Aspergillus niger, Aspergillus oryzae, yeasts, some species from the Lactobacillus genus and others. [7] b-Galactosidases from microorganisms have attracted considerable attention because of their use in biotechnological applications.…”

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confidence: 99%

Characterization of a thermostable recombinant β-galactosidase from a thermophilic anaerobic bacterial consortium YTY-70

Liu

Zhao

Deng

et al. 2015

Biotechnology & Biotechnological Equipment

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In the present study, a thermophilic anaerobic bacterial consortium YTY-70 that produced thermostable b-galactosidase was isolated from a hot spring in Yongtai (Fujian, China). Based on 16S rRNA sequences, we concluded that Caldicellulosiruptor was the predominant genus in the studied bacterial consortium. Subsequently, a thermostable b-galactosidase gene was cloned and expressed in Escherichia coli as a fusion protein with glutathione S-transferase. The recombinant enzyme exhibited a maximum activity at an optimum pH of 7.0 and an optimum temperature of 75 C. It had a high activity across a broad pH range (between pH 5.0 and pH 9.0) and high thermal stability at temperatures up to 90 C. The activity of the recombinant b-galactosidase was enhanced by TritonX-100, Tween-20 and 1 mmol/L 2-mercaptoethanol, while it was inhibited by ethylenediaminetetraacetic acid, sodium dodecyl sulphate, phenylmethylsulphonyl fluoride and 10 mmol/L 2-Me. The enzyme's catalytic function was enhanced by the following metal ions: Na C , K Fe 3C and Li C . The thermostable b-galactosidase might be a promising candidate for use in food industries, particularly for the dairy industry and biosynthesis of galacto-oligosaccharides, due to its high thermostability and broad pH range.

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“…Enzymatic hydrolysis of lactose by β-galactosidase is one of the most popular technologies to produce lactose reduced/free milk and related dairy products for consumption by lactose intolerant people [8][9][10][11][12][13]. Additionally, Lactosehydrolysed milk used for the preparation of yoghurt and cheese manufactory accelerate the acidification process that reduces the set time of yoghurt and develop the structure and flavor in cheese [14]. β-Galactosidases are found in microorganisms (bacteria, fungi, yeasts), plants especially in almonds, peaches, apricots, apples and animal organs [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Extraction, Purification and Characterization of Apricot Seed β-Galactosidase for Producing Free Lactose Cheese

Yossef¹

2014

J Nutr Food Sci

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Abstractβ-Galactosidase was extracted (with acetate buffer pH 5) from apricot seeds, partially purified by ammonium sulphate (30-70%) and dialyzed for 24 hr. The crude extract had a higher specific activity (9.93 U/mg proteins) which indicates a high enzyme yield. Purification of crude extract with ammonium sulphate (30-70%) increased the specific activity and purification fold to 29.07 U/mg proteins and 2.92, respectively which was improved by dialysis to 32.68 U/mg proteins and 3.29, respectively. The extracted enzyme exhibits an optimum temperature at 70°C and 5 pH optima. The enzyme activity was almost stable between pH 5.0 and 6.5, where more than 90% of its activity was remained with incubation at the previous pH for 30 min. Further more; it was thermostable when incubated for 30 min. at temperature ranges of 55-70°C with a complete loss of activity at 80°C. The activity of β-galactosidase was enhanced by different concentration of Ca +2 . There were no significant (P>0.05) changes in flavor, body texture, and overall acceptability between free lactose white cheese treated by apricot seeds β -galactosidase (9865 U/ 500 ml milk) and untreated cheese.

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Beta‐galactosidase technology: A solution to the lactose problem

Cited by 124 publications

References 80 publications

Whey, a Potential Substrate for Biotechnology

Whey, a Potential Substrate for Biotechnology

Characterization of a thermostable recombinant β-galactosidase from a thermophilic anaerobic bacterial consortium YTY-70

Extraction, Purification and Characterization of Apricot Seed β-Galactosidase for Producing Free Lactose Cheese

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