Hydrolysis of whey lactose by immobilized β-galactosidase in a bioreactor with a spirally wound membrane

Vasileva, N.; Ivanov, Yavor; Damyanova, Stanka; Kostova, Iliana; Godjevargova, Tzonka

doi:10.1016/j.ijbiomac.2015.11.025

Cited by 40 publications

(17 citation statements)

References 31 publications

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“…1,6‐Hexamethylenediamine (1,6‐HMDA), 3‐aminopropyltriethoxysilane (APTES) and 1,12‐diaminododecane are the frequently used modification reagents to generate s membrane amino group, which can react with the carboxy group of the enzyme molecule or further conjugate with other modifiers. In reality, the three reagents are usually used in combination with glutaraldehyde (GLU) to achieve a biocatalytic membrane.…”

Section: The Fouling‐like Immobilizationsmentioning

confidence: 99%

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Immobilization of Enzymes in/on Membranes and their Applications

et al. 2019

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Enzyme membrane reactors (EMRs) are becoming increasingly interesting for application in bioconversion processes in food processing, pharmaceutics, biorefinery and wastewater treatment. Integrating the highly efficient enzymatic reaction with selectable membrane separation technology, the EMRs are able to reduce product inhibition, improve the stability of the enzyme, increase the number of reaction cycles and sustainably separate products from biotransformation solutions. Generally, in EMRs, enzymes can be either free in the solution, immobilized on an additional carrier or immobilized directly in/on a porous structure of the membrane, of which the system with the enzyme immobilized directly in/on the membrane (EIM) is a relatively simple and most widely applied method. The EIM system not only facilitates recycling of the enzymes but also in many cases additionally enhances enzyme properties such as the stability and viability. A membrane with a porous structure is usually considered as a potential carrier for enzyme immobilization. A series of immobilization methods has been developed to fix the enzymes on the membranes. The purpose of this review is to systemically summarize the immobilization methods of enzymes in/on membranes and the applications of the EIM system for biocatalysis.

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Section: The Fouling‐like Immobilizationsmentioning

confidence: 99%

“…1,6‐HMDA acts in a similar way when applied to immobilize β‐galactosidase (β‐Gal). The porous polypropylene membrane is firstly modified with 1,6‐HMDA to convert the carboxy groups into amino groups . Subsequently, the β‐Gal is covalently immobilized onto the membrane via GLU.…”

Section: The Fouling‐like Immobilizationsmentioning

confidence: 99%

Immobilization of Enzymes in/on Membranes and their Applications

et al. 2019

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“…Industries prefer to hydrolyse lactose using free enzyme however, the immobilization of β-galactosidase begins to draw the attention of producers. The ability to efficiently hydrolyse whey lactose is one of the key factors determining overall process economy (Vasileva et al, 2016). The aim of this study was to investigate β-galactosidase preparates for fermentation capability using concentrated whey and milk permeates with 20, 30 and 40% (w w -1 ) of total solids.…”

Section: Introductionmentioning

confidence: 99%

Lactose hydrolysis in different solids content whey and milk permeates

Zolnere¹,

Ciproviča²

2019

Foodbalt

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Dairy permeates contain almost original amount of lactose, small fraction of other solid compounds and water. For complete lactose hydrolysis and glucose-galactose syrup production, it is essential to ensure the optimal substrate concentration and conditions to improve product quality and save energy, water and material costs. The aim of this study was to investigate β-galactosidase preparates capability using concentrated whey and milk permeates with 20, 30 and 40% (w w-1) of total solids. Commercial β-galactosidase preparates (Ha-Lactase 5200 produced by Kluyveromyces lactis and NOLA Fit5500 produced by Bacillus licheniformis, Chr.HANSEN; GODO-YNL2 produced by Kluyveromyces lactis, Danisco, Denmark) at dosage 500 NLU•L-1 (Ha-Lactase 5200, GODO-YNL2) and 500 BLU•L-1 (NOLA Fit5500) were used for lactose hydrolysis. The concentration of each permeate was 20, 30 and 40% (w w-1) of total solids. 10% KOH was used to adjust optimal pH for fermentation media. Samples were monitored in incubator for 4 hours at temperature 42.5±0.5 °C. Lactose, glucose and galactose concentrations were determined by HPLC (Shimadzu LC-20 Prominence, USA). Ha-Lactase 5200 preparate was able to increase lactose hydrolysis rate more than 90% in all permeates at 20% and 30% solids concentration. GODO-YNL2 preparate showed the highest conversion of glucose in sweet whey permeate at 20% solids concentration and the lowest conversion of galactose in sweet whey permeate at 30% solids concentration. The results indicated that substrate type and solids concentration have an effect on the relative activity of commercial enzymes. The study results give a greater understanding about permeates suitability for glucose-galactose syrup production.

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“…During the last three decades, the application of β-galactosidase for hydrolysis of lactose in the dairy industries increased. The enzyme was used to improve the technological and sensorial characteristics of dairy products: produce lactose-free milk or fermented products, which is a suitable approach for treating individuals suffering from lactose intolerance affecting humans worldwide (Vasileva et al, 2016;Harju et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

Ibrahim

2018

Emir J Food Agric

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It is known that, the main problem associated with the production of fermented camel milk is the lower growth rate of lactic acid bacteria which caused many quality problems in the final product. The aim of this research was to enhance of β-galactosidase enzymatic activity of Lactobacillus delbrueckii ssp. bulgaricus DSMZ 20081, Streptococcus thermophilus ATCC 19258 and Lactobacillus acidophilus DSMZ 20079 by cell-rupture method to release their intracellular β-galactosidase and used the ruptured cell cultures as the source of the β-galactosidase enzyme. The results show that the bacterial growth rate in fermented camel milk made by using mixed cells of L. delbrueckii ssp. bulgaricus, S. thermophilus and L. acidophilus was 2 h faster than whole cells of the same strains. Moreover, the significant (P<0.05) faster dropping in pH-value to about 4.6 was observed in fermented camel milk made by using mixed cells of S. thermophilus, L. acidophilus and L. delbrueckii ssp. bulgaricus it was 4.65±0.02, 4.64±0.01and 4.63±0.01 during 4 h of fermentation time, respectively. Furthermore, the highest significance (P<0.05) activity of β-galactosidase was obtained during 4 h of fermentation in all fermented camel milk made by using mixed cells of L. delbrueckii ssp. bulgaricus, L. acidophilus and S. thermophilus it was about 1.97±0.12, 1.77±0.06 and 1.70±0.01 IU/ml, respectively. On the other hand, more rapid and efficient utilization of lactose was observed in fermented camel milk made by using mixed cells of S. thermophilus, L. acidophilus and L. delbrueckii ssp. bulgaricus during the first 2 h of incubation time and the higher degree of lactose hydrolysis reached the maximum approximately 37.69, 38.39 and 40.56 % at the end of 10h of incubation time, respectively. The present results revealed that enhance of microbial growth rate in fermented camel milk can be simultaneously achieved by a suitable rupture-cell method.

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Hydrolysis of whey lactose by immobilized β-galactosidase in a bioreactor with a spirally wound membrane

Cited by 40 publications

References 31 publications

Immobilization of Enzymes in/on Membranes and their Applications

Immobilization of Enzymes in/on Membranes and their Applications

Lactose hydrolysis in different solids content whey and milk permeates

ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

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