Milk lactose removal by β-galactosidase immobilized on eggshell membrane

Kızıldağ, Selen; Işık, Ceyhun; Teke, Mustafa

doi:10.1007/s00217-023-04280-3

Cited by 5 publications

(3 citation statements)

References 43 publications

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“…Protease (Novo-Pro D) immobilised on agarose activated with a glyoxyl group was used to hydrolyse casein ten times without any decrease in activity [60]. Others have also reported multiple reuses of enzymes immobilised covalently [16,61,62].…”

Section: Chemical Methods Of Enzyme Immobilisation 221 Covalent Bondmentioning

confidence: 99%

The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

Alzahrani,

Akanbi,

Scarlett

et al. 2024

Processes

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The use of edible oils and fats in dairy products is becoming increasingly important in the food industry because of their complementary functional properties. Most of these products are produced using food-grade enzymes as processing aids because processes involving enzymes are considered mild and environmentally friendly for regulatory purposes. The poor stability and recovery of enzymes in their native state limit their performance, and to enhance their activity, stability, and reusability, enzymes are often immobilised—a process that involves attaching them to a solid support. Additionally, immobilisation enables enzymes to selectively target specific substrates or products, making them highly efficient. These features have led to the increased use of immobilised enzymes in dairy and lipid processing and enzymes have been used to produce a broad range of products such as whey protein concentrates and isolates, peptide–lipid conjugates, lipid concentrates, structured lipids, and human milk fat substitutes. Therefore, this article reviews the current progress on different enzyme preparations and their use in lipid and dairy processing. It also summarises opportunities in enzyme-catalysed valorisation of dairy and lipid waste streams with the ultimate goals of sustainable food production and reductions in waste.

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Section: Chemical Methods Of Enzyme Immobilisation 221 Covalent Bondmentioning

confidence: 99%

The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

Alzahrani,

Akanbi,

Scarlett

et al. 2024

Processes

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“…As model enzymes, we have used Eversa Transform 2.0 (EVR), a very stable lipase that is commercially available, which has been prepared by genetic modification of the lipase from Thermomyces lanuginosus − and the β-galactosidase from Aspergillus oryzae as an enzyme showing a lower stability. − Although the enzymes have been chosen just as a model system, we can envisage some joint applications of both enzymes. One likely application may be the simultaneous modification of the fats and lactose of milk to produce free-lactose milk (or lactose enriched in prebiotic galactosides) − that could also bear flavors produced by the lipase action, decrease the triglyceride concentration, − or be protected by the presence of some free fatty acids with antimicrobial agent activity. − Other application may be the production of galactosyl-diglycerides using lipase to produce specific diglycerides from the corresponding triglyceride (e.g., 1,2 diacetin) and the β-galactosidase from A. oryzae as the catalyst to produce the O-link ,− between galactose and diglyceride via kinetically controlled synthesis. − In this instance, the high concentration inside the particle of the diglyceride may be critical to have good reaction yields, and the immediate modification can prevent the fact that the acyl migration results in 1,3 diacetin …”

Section: Introductionmentioning

confidence: 99%

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated

Carballares,

Abellanas-Perez,

de Andrades

et al. 2024

ACS Sustainable Chem. Eng.

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In the present article, glutaraldehyde was used to covalently coimmobilize the lipase Eversa Transform 2.0 and the β-galactosidase from Aspergillus oryzae. Both enzymes were adsorbed on amino supports and modified with glutaraldehyde. However, the first enzyme remained almost fully active under stress conditions, while the β-galactosidase lost a large percentage of its activity. To prevent the necessity of discarding both enzymes, the lipase was covalently immobilized following this immobilization strategy. The biocatalyst was reduced to eliminate its chemical reactivity, and the β-galactosidase was then coimmobilized via ion exchange. The incubation at high concentrations of salt desorbed the β-galactosidase from the support. This combi-biocatalyst was used in three inactivation/rebuilding cycles where the inactivated β-galactosidase was liberated from the combi-biocatalyst by washing at high ionic strength and replaced with a fresh enzyme, while the immobilized lipase maintained its activity throughout the 3 cycles. That way, it was possible to use this strategy to reuse the immobilized Eversa Transform 2.0 to build new combi-biocatalysts after β-galactosidase inactivation.

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“…With the development of lactose removal technologies, the main challenge for manufacturers is to prepare low-lactose/lactose-free dairy products that are consistent with or exceed traditional dairy products in nutrition, flavor, and quality. Processing technologies and conditions are continuously being innovated, for example, studies reported characterization strains [ 10 ] of high yield and materials of immobilized lactase [ 11 ], coupling membrane, co-fermentation, etc. In this paper, the epidemiology and pathology of lactose intolerance are briefly introduced.…”

Section: Introductionmentioning

confidence: 99%

Advances in Low-Lactose/Lactose-Free Dairy Products and Their Production

Zheng

Han

et al. 2023

Foods

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With increasing health awareness worldwide, lactose intolerance has become a major concern of consumers, creating new market opportunities for low-lactose/lactose-free dairy foods. In recent years, through innovating processes and technologies, dairy manufacturers have significantly improved the variety, and functional and sensory qualities of low-lactose and lactose-free dairy products. Based on this, this paper first covers the pathology and epidemiology of lactose intolerance and market trends. Then, we focus on current advantages and disadvantages of different lactose hydrolysis technologies and improvements in these technologies to enhance nutritional value, and functional, sensory, and quality properties of lactose-free dairy products. We found that more and more cutting-edge technologies are being applied to the production of lactose-free dairy products, and that these technologies greatly improve the quality and production efficiency of lactose-free dairy products. Hopefully, our review can provide a theoretical basis for the marketing expansion and consumption guidance for low-lactose/lactose-free dairy products.

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Milk lactose removal by β-galactosidase immobilized on eggshell membrane

Cited by 5 publications

References 43 publications

The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated

Advances in Low-Lactose/Lactose-Free Dairy Products and Their Production

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