β-galactosidase as an industrial enzyme: production and potential

Singh, Rahul Vikram; Sambyal, Krishika

doi:10.1007/s11696-022-02507-3

Cited by 12 publications

(9 citation statements)

References 131 publications

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“…Such an increased affinity could be regarded to the conformational alterations that occurred in the iβ-GL as these conformational alterations could have promoted the substrate accessibility to the active site 43 . Noteworthy, lactose is the substrate involved in variable β-GL applications, such as whey valorization, preparation of the prebiotic galacto-oligosaccharides, and preparation of low lactose or lactose free dairy products 14 . Thus, the GA-PP-Carr iβ-GL increased affinity to lactose would encourage its exploitation in these industrial applications.…”

Section: Resultsmentioning

confidence: 99%

“…The free and the GA-PP-Carr iβ-GLs stabilities were assessed in presence of Ca 2+ , Al 3+ , SDS, and EDTA. β-GLs were reported to be inhibited via Calcium ions 14 . Calcium is the chief milk mineral and it is also present in whey.…”

Section: Resultsmentioning

confidence: 99%

“…Calcium is the chief milk mineral and it is also present in whey. Two thirds of milk calcium form complexes with casein 48 .Thus, they may not interact with or inhibit β-GL 14 . However, the remaining third of milk calcium is in serum phase.…”

Section: Resultsmentioning

confidence: 99%

“…Lactose degradation via β-GL would provide the low lactose or the lactose free dairy products which are crucial for lactose-intolerant people. Reducing lactose would also reduce crystallization, and this would boost the smoothness of variable dairy products, such as cheese, curd, and ice-cream 14 . Whey, a byproduct of dairy industries, could also be subjected to β-GL mediated lactose degradation.…”

Section: Introductionmentioning

confidence: 99%

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Glutaraldehyde-pea protein grafted polysaccharide matrices for functioning as covalent immobilizers

Wahba

2023

Sci Rep

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Three polysaccharide matrices (κ-Carrageenan (Carr), gellan gum, and agar) were grafted via glutaraldehyde (GA) and pea protein (PP). The grafted matrices covalently immobilized β-d-galactosidase (β-GL). Nonetheless, grafted Carr acquired the topmost amount of immobilized β-GL (iβ-GL). Thus, its grafting process was honed via Box-Behnken design and was further characterized via FTIR, EDX, and SEM. The optimal GA-PP-Carr grafting comprised processing Carr beads with 10% PP dispersion of pH 1 and 25% GA solution. The optimal GA-PP-Carr beads acquired 11.44 Ug−1 iβ-GL with 45.49% immobilization efficiency. Both free and GA-PP-Carr iβ-GLs manifested their topmost activity at the selfsame temperature and pH. Nonetheless, the β-GL Km and Vmax values were reduced following immobilization. The GA-PP-Carr iβ-GL manifested good operational stability. Moreover, its storage stability was incremented where 91.74% activity was offered after 35 storage days. The GA-PP-Carr iβ-GL was utilized to degrade lactose in whey permeate with 81.90% lactose degradation efficiency.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glutaraldehyde-pea protein grafted polysaccharide matrices for functioning as covalent immobilizers

Wahba

2023

Sci Rep

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“…3.2.1.23) which hydrolyses terminal non-reducing β-D-galactose residues in β-D-galactosides. This enzyme (LacZ) is one of the most thoroughly characterized enzymes: the protein played a central role in Jacob and Monod’s development of the operon model for the regulation of gene expression [ 1 ] and belongs to a significant food industrial enzyme family utilized in the production of lactose-free dairy products [ 2 ]. E. coli is often preferred as an indicator organism to assess fecal contamination of food and water, however, LacZ activity can reflect the concentration of cells and β-galactosidase is often used generally as a marker for coliforms [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Physiologically Aggregated LacZ Applied in Trehalose Galactosylation in a Recycled Batch Mode

Belkova,

Janegova,

Hrabarova

et al. 2023

Life

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Galactooligosaccharides obtained via β-galactosidase transgalactosylation have health-promoting properties and are widely recognized as effective prebiotics. Trehalose-based galactooligosaccharides could be introduced into food and pharmaceutical industries similarly to trehalose. In light of this, new technological approaches are needed. Recently, in vivo enzyme immobilizations for recombinant proteins have been introduced, and physiological aggregation into active inclusion bodies (aIBs) has emerged as one such method of in vivo immobilization. To prepare LacZ β-galactosidase in the form of aIBs, we used a short 10 amino acid aggregation-prone tag. These native protein particles were simply washed from the cell lysate and applied in trehalose galactosylation in a recycled batch mode. In this study, aIBs entrapped in alginate beads, encapsulated in alginate/cellulose sulfate/poly(methylene-co-guanidine) capsules and magnetized were compared with free aIBs. Alginate/cellulose sulfate/PMCG capsules showed more suitable properties and applicability for biotransformation of trehalose at its high concentration (25%, w/v) and elevated temperature (50 °C).

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