Immobilization of Aspergillus oryzae β-galactosidase in cation functionalized agarose matrix and its application in the synthesis of lactulose

Serey, Marcela; Vera, Carlos; Guerrero, Cecilia; Illanes, Andrés

doi:10.1016/j.ijbiomac.2020.11.110

Cited by 20 publications

(6 citation statements)

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“…A. oryzae lactase was immobilized by the ionic mechanism in a quaternary ammonium agarose support. The biocatalyst obtained showed the highest GOS yield and specific productivity values of 24 % (w/w) and 9.78 g•g −1 h −1 , respectively [59]. In this study, the cumulative weight of generated oligosaccharides was higher under repeated batch mode with immobilized β-galactosidase than the value obtained with a soluble enzyme under single batch mode.…”

Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 50%

“…Different functionalized mesoporous supports, biopolymers and nanoparticles have been employed. A commercial preparation of lactase extracted from A. oryzae was covalently immobilized [59] by using amino-glyoxyl-agarose as support, the maximum GOS obtained was approximately 5% [55]. However, the GOS yield by transgalactosylation activity was 20% when the same β-galactosidase was immobilized on glyoxyl-functionalized porous silica support, whereas the yield of the free enzyme form was only 11% [60].…”

Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 99%

“…Due to the structure and distribution of residual amino acid of A. oryzae β-galactosidase, protein immobilization by ionic interaction is possible [59]. The essential advantages of this fast and easy immobilization procedure are that no additional reagents or modifications of the enzyme are needed.…”

Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 99%

See 2 more Smart Citations

Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities

Liburdi

Esti

2022

Beverages

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Much attention has recently been paid to β-Galactosidases (β-D-galactoside galactohidrolase; EC 3.2.1.23), commonly known as lactases, due to the lactose intolerance of the human population and the importance of dairy products in the human diet. This enzyme, produced by microorganisms, is being used in the dairy industry for hydrolyzing the lactose found in milk to produce lactose-free milk (LFM). Conventionally, β-galactosidases catalyze the hydrolysis of lactose to produce glucose and galactose in LFM; however, they can also catalyze transgalactosylation reactions that produce a wide range of galactooligosaccharides (GOS), which are functional prebiotic molecules that confer health benefits to human health. In this field, different works aims to identify novel microbial sources of β-galactosidase for removing lactose from milk with the relative GOS production. Lactase extracted from thermophilic microorganisms seems to be more suitable for the transgalactosylation process at relatively high temperatures, as it inhibits microbial contamination. Different immobilization methods, such as adsorption, covalent attachment, chemical aggregation, entrapment and micro-encapsulation, have been used to synthesize lactose-derived oligosaccharides with immobilized β-galactosidases. In this mini-review, particular emphasis has been given to the immobilization techniques and bioreactor configurations developed for GOS synthesis in milk, in order to provide a more detailed overview of the biocatalytic production of milk oligosaccharides at industrial level.

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Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 50%

Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 99%

Section: Recent Advances In β-Galactosidase Immobilization For Gos Pr...mentioning

confidence: 99%

See 1 more Smart Citation

Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities

Liburdi

Esti

2022

Beverages

View full text Add to dashboard Cite

show abstract

“…β-Galactosidase, commonly known as lactase (EC 3.2.1.23), is widely used in the food industry to improve the sweetness, solubility, and flavor of dairy products (Oliveira at al., 2011;Saqib et al, 2017). The commercially used β-galactosidases are mainly from Aspergillus oryzae and Kluyveromyces lactis (Horiuchi et al, 2009;Husain, 2010;Saqib et al, 2017;Serey et al, 2021). Many bacterial strains also have the capacity to produce β-galactosidases, including Bifidobacterium longum, Bacillus circulans, and Lactobacillus spp.…”

Section: Introductionmentioning

confidence: 99%

Site-directed mutation of β-galactosidase from Streptococcus thermophilus for galactooligosaccharide-enriched yogurt making

Zhao

et al. 2022

Journal of Dairy Science

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β-Galactosidase is one of the most important enzymes used in dairy processing. It converts lactose into glucose and galactose, and also catalyzes galactose to form galactooligosaccharides (GOS), so-called prebiotics. However, most of the β-galactosidases from the starter cultures have low transgalactosylation activities, the process that results in galactose accumulation in yogurt. Here, a site-directed mutation strategy was attempted, to genetically modify β-galactosidase from Streptococcus thermophilus. Out of 28 Strep. thermophilus strains, a β-galactosidase gene named bgaQ, encoded for high β-galactosidase hydrolysis activity (BgaQ), was cloned from the strain Strep. thermophilus SDMCC050237. It was 3,081 bp in size, with 1,027 deduced amino acid residuals, which belonged to the GH2 family. After replacing the Tyr 801 and Pro 802 around the active sites of BgaQ with His 801 and Gly 802 , the GOS synthesis of the generated mutant protein BgaQ-8012 increased from 20.5% to 26.7% at 5% lactose, and no hydrolysis activity altered obviously. Subsequently, the purified BgaQ or BgaQ-8012 was added to sterilized milk inoculated with 2 starters from Strep. thermophilus SDMCC050237 and Lactobacillus delbrueckii ssp. bulgaricus ATCC11842. The GOS yields with added BgaQ or BgaQ-8012 increased to 5.8 and 8.3 g/L, respectively, compared with a yield of 3.7 g/L without enzymes added. Meanwhile, the addition of the BgaQ or BgaQ-8012 reduced the lactose content by 49.3% and 54.4% in the fermented yogurt and shortened the curd time. Therefore, this study provided a site-directed mutation strategy for improvement of the transgalactosylation activity of β-galactosidase from Strep. thermophilus for GOS-enriched yogurt making.

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“…This is crucial for enzymes for industrial use, where having a biocatalyst with good catalytic performance must be balanced with the economic viability of the process. This is the case of β-galactosidase (β-gal), a well-known enzyme with wide applications in the production of lactose-free products or prebiotics, such as galacto-oligosaccharide (GOS), lactulose and other syrups [ 17 , 18 , 19 , 20 ]. The need to improve the economic and catalytic performance of β-galactosidases for industrial application has driven the development of numerous immobilization strategies [ 21 ].…”

Section: Introductionmentioning

confidence: 99%

Development of a Hybrid Bioinorganic Nanobiocatalyst: Remarkable Impact of the Immobilization Conditions on Activity and Stability of β-Galactosidase

et al. 2021

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Hybrid bioinorganic biocatalysts have received much attention due to their simple synthesis, high efficiency, and structural features that favor enzyme activity and stability. The present work introduces a biomineralization strategy for the formation of hybrid nanocrystals from β-galactosidase. The effects of the immobilization conditions were studied, identifying the important effect of metal ions and pH on the immobilization yield and the recovered activity. For a deeper understanding of the biomineralization process, an in silico study was carried out to identify the ion binding sites at the different conditions. The selected β-galactosidase nanocrystals showed high specific activity (35,000 IU/g biocatalyst) and remarkable thermal stability with a half-life 11 times higher than the soluble enzyme. The nanobiocatalyst was successfully tested for the synthesis of galacto-oligosaccharides, achieving an outstanding performance, showing no signs of diffusional limitations. Thus, a new, simple, biocompatible and inexpensive nanobiocatalyst was produced with high enzyme recovery (82%), exhibiting high specific activity and high stability, with promising industrial applications.

show abstract

Immobilization of Aspergillus oryzae β-galactosidase in cation functionalized agarose matrix and its application in the synthesis of lactulose

Cited by 20 publications

References 49 publications

Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities

Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities

Site-directed mutation of β-galactosidase from Streptococcus thermophilus for galactooligosaccharide-enriched yogurt making

Development of a Hybrid Bioinorganic Nanobiocatalyst: Remarkable Impact of the Immobilization Conditions on Activity and Stability of β-Galactosidase

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