Statistical Modeling of β-galactosidase Inhibition During Lactose Hydrolysis

Boyaci, İsmail Hakkı; Baş, Deniz; Dudak, Fahriye Ceyda; Topçu, Ali; Saldamlı, İlbilge; Şeker, Urartu Özgür Şafak; Tamerler, Candan

doi:10.1080/08905430500524267

Cited by 6 publications

(2 citation statements)

References 13 publications

(18 reference statements)

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“…Therefore, the desirable enzymes are those with low inhibition of lactose hydrolysis by glucose. The inhibitory or activator effects of glucose and galactose are also dependent on the enzyme source and on the concentration of reagents and products (170). Hence, β-galactosidase from Kluyveromyces fragilis was reported to be affected by both combined and individual effects of lactose, glucose and galactose.…”

Section: Gosmentioning

confidence: 99%

Technological Aspects of the Production of Fructo and Galacto-Oligosaccharides. Enzymatic Synthesis and Hydrolysis

et al. 2019

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Fructo- and galacto-oligosaccharides (FOS and GOS) are non-digestible oligosaccharides with prebiotic properties that can be incorporated into a wide number of products. This review details the general outlines for the production of FOS and GOS, both by enzymatic synthesis using disaccharides or other substrates, and by hydrolysis of polysaccharides. Special emphasis is laid on technological aspects, raw materials, properties, and applications.

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Section: Gosmentioning

confidence: 99%

Technological Aspects of the Production of Fructo and Galacto-Oligosaccharides. Enzymatic Synthesis and Hydrolysis

et al. 2019

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“…Depending on the β-galactosidase isolation source and reaction conditions, the kinetics based on the Michaelis-Menten model or product inhibition can be found. In the second case, glucose, galactose, as well as mixed inhibition, is possible [18][19][20][21][22]. The most common strategy is related to competitive galactose inhibition (Equation ( 1)).…”

Section: Introductionmentioning

confidence: 99%

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

Czyżewska

Trusek-Hołownia

2021

Catalysts

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The current requirements of industrial biocatalysis are related to economically beneficial and environmentally friendly processes. Such a strategy engages low-temperature reactions. The presented approach is essential, especially in food processes, where temperature affects the quality and nutritional value foodstuffs. The subject of the study is the hydrolysis of lactose with the commercial lactase NOLA™ Fit 5500 (NOLA). The complete decomposition of lactose into two monosaccharides gives a sweeter product, recommended for lactose intolerant people and those controlling a product’s caloric content. The hydrolysis reaction was performed at 15 °C, which is related to milk transportation and storage temperature. The enzyme showed activity over the entire range of substrate concentrations (up to 55 g/L lactose). For reusability and easy isolation, the enzyme was encapsulated in a sodium alginate network. Its stability allows carrying out six cycles of the complete hydrolysis of lactose to monosaccharides, lasting from two to four hours. During the study, the kinetic description of native and encapsulated NOLA was conducted. As a result, the model of competitive galactose inhibition and glucose mixed influence (competitive inhibition and activation) was proposed. The capsule size does not influence the reaction rate; thus, the substrate diffusion into capsules can be omitted from the process description. The prepared 4 mm capsules are easy to separate between cycles, e.g., using sieves.

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Improvement of functional properties of a thermostable β‐glycosidase for milk lactose hydrolysis

et al. 2018

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In this work, a new exploitation of the thermostable β-glycosidase from Sulfolobus solfataricus expressed in Saccharomyces cerevisiae to create functional foods for low lactose diets was evaluated. For this purpose, the lactose hydrolysis reaction using immobilized and soluble enzymes was investigated. Activity and stability at different conditions of pH and temperature were tested. The immobilization process had a big impact on the catalysis performance, leading to an enhancement of the enzymatic reaction rate on lactose, as demonstrated by the increasing of 2 and 2.5 folds of K and K /K , respectively. Moreover, the maximal activity for the immobilized form was referred at pH 6.5 instead of 7.0, leading to an improvement of the catalytic performance at milk pHs. Although the soluble enzyme was already weakly inhibited by the reaction products, the immobilization further reduced the inhibitory action of glucose increasing the K from 96.7 to 110.4 mM. Finally, the immobilized enzyme showed high hydrolysis rate in whole milk that yielded 99% of lactose breakdown in 10 and 30 min at 60 and 40°C, respectively. These results support the application of the immobilized β-glycosidase for the development of new functional foods particularly suitable to the alleviation of lactose intolerance.

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Statistical Modeling of β-galactosidase Inhibition During Lactose Hydrolysis

Cited by 6 publications

References 13 publications

Technological Aspects of the Production of Fructo and Galacto-Oligosaccharides. Enzymatic Synthesis and Hydrolysis

Technological Aspects of the Production of Fructo and Galacto-Oligosaccharides. Enzymatic Synthesis and Hydrolysis

Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature

Improvement of functional properties of a thermostable β‐glycosidase for milk lactose hydrolysis

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