Characterization and Application of a New β-Galactosidase Gal42 From Marine Bacterium Bacillus sp. BY02

Zhou, Zihan; He, Ningning; Han, Qiang; Liu, Songshen; Xue, Ruikun; Hao, Jianhua; Li, Shangyong

doi:10.3389/fmicb.2021.742300

Cited by 8 publications

(3 citation statements)

References 36 publications

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“…The LacLM heterodimeric Lactobacillus acidophilus R22 β-galactosidase was activated by Mg 2+ which improved both activity and stability suggesting the possible presence of binding sites for Mg 2+ within the active site which might interact with Glu residues and, thus, could contribute to both subunit interactions and global enzyme stabilization. 9,46 Chitin is insoluble in water and organic solvents but could be processed by extensive alkaline deacetylation to obtain a more soluble product called chitosan. The chitin yield from the Achatina shells was 74.64%, while the chitosan yield was 58.60%.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

2024

TJNPR

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Most GOS are classified as prebiotic food (since they are nondigestible) or Bifidus growth factor as they can stimulate the establishment of human colonic Bifidobacteria species. In addition, GOS, by suppressing the expression of bacterial quorum-sensing (QS) genes, could prevent the growth and production of biofilms by some possible harmful enteric bacteria. [10][11][12][13] Industrial β-galactosidases are usually sourced from microorganisms, especially fungi, bacteria, and yeasts. 8,9,14 Although many bacteria produce β-galactosidases, major β-galactosidase production has majorly focused on the use of some Lactobacillus species of the Lactic acid bacteria (LBA) with the "Generally Regarded As Safe (GRAS)" status. 15,16 LBA is naturally found in any environment rich in carbohydrates, such as decomposing plant materials, fermented foods, and in the feces of individuals on high milk, lactose, or dextrin diets. 17 Lactobacillus acidophilus ('acid-loving milk-bacillus') is a homofermentative species of Lactobacillus that grows at pH below 5.0 in the lumen of the gut, especially the lower end of the small intestine where it metabolizes any residual lactose, thus encouraging lactose digestion in individuals with low galactosidase activity. 15 Good thermostability and cost are major factors to consider in the industrial application of enzymes. 18 At higher temperatures, thermostable enzymes have increased activity, substrates maintain higher solubility and microbial fouling could be considerably reduced. 9 High cost is a critical issue in the industrial use of immobilized enzymes in relation to enzyme reusability and the regenerability of immobilization supports. This issue has been sufficiently addressed by the overwhelming choice of biopolymeric immobilization supports like some proteins and carbohydrates, but more especially the polysaccharides, chitin, and chitosan. [19][20][21] Chitin is one of the most abundant natural polymers. It can be easily obtained at a relatively low

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Section: Resultsmentioning

confidence: 99%

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

2024

TJNPR

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“…The activity of β-gal can be estimated by liberating O-nitrophenol (ONP) from O-nitrophenyl-β-D-galactopyranoside (ONPG) as a substrate according to the method characterized by Zhou et al [ 22 ] with some modifications. The reaction was started by adding 0.1 ml of the enzyme solution (in the case of a free enzyme) or 0.1 g of beads (in the case of an immobilized enzyme) to 0.9 ml of 10 mM ONPG solution prepared in phosphate buffer (0.1 M, pH 7.0).…”

Section: Methodsmentioning

confidence: 99%

Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Abdella,

Hassan

2024

Bioprocess Biosyst Eng

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Abstractβ-galactosidase has been immobilized onto novel alginate/tea waste gel beads (Alg/TW) via covalent binding. Alg/TW beads were subjected to chemical modification through amination with polyethyleneimine (PEI) followed by activation with glutaraldehyde (GA). Chemical modification parameters including PEI concentration, PEI pH, and GA concentration were statistically optimized using Response Surface methodology (RSM) based on Box–Behnken Design (BBD). Analysis of variance (ANOVA) results confirmed the great significance of the model that had F value of 37.26 and P value < 0.05. Furthermore, the R2 value (0.9882), Adjusted R2 value (0.9617), and predicted R2 value (0.8130) referred to the high correlation between predicted and experimental values, demonstrating the fitness of the model. In addition, the coefficient of variation (CV) value was 2.90 that pointed to the accuracy of the experiments. The highest immobilization yield (IY) of β-galactosidase (75.1%) was given under optimized conditions of PEI concentration (4%), PEI pH (9.5), and GA concentration (2.5%). Alg/TW beads were characterized by FT-IR, TGA, and SEM techniques at each step of immobilization process. Moreover, the immobilized β-galactosidase revealed a very good reusability as it could be reused for 15 and 20 consecutive cycles keeping 99.7 and 72.1% of its initial activity, respectively. In conclusion, the environmental waste (tea waste) can be used in modern technological industries such as the food and pharmaceutical industry.

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“…EDTA was also shown to inhibit the activity of β-galactosidases from B. infantis and Bacillus sp. BY02 (Hung and Lee, 2002;Zhou et al, 2021).…”

Section: Cationmentioning

confidence: 99%

Evaluation of transgalactosylation activity of commercial β-galactosidase from Bifidobacterium bifidum for synthesis of prebiotic oligosaccharides

Milano,

Arreola

2023

IFRJ

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Galacto-oligosaccharides (GOS) are products of transgalactosylation reaction of β-galactosidase when lactose is used as the substrate. These carbohydrates are considered prebiotics which stimulate beneficial effects to human health. In the present work, Saphera, a commercial preparation of β-galactosidase from Bifidobacterium bifidum, was biochemically characterised for production of GOS. Using o-nitrophenyl-β-D-galactopyranoside (oNPG) as the substrate, optimal activity for the enzyme was found to be at pH 6.0 and at 45°C. Ten (10) mM each of either Na+ or K+ enhanced enzyme activity by 10%, while Cu2+, Zn2+, Fe2+, and EDTA showed inhibitory effect on the enzyme activity. When incubated in 50 mM sodium phosphate and pH 6.5, the enzyme was found to have half-life time of 136 ± 6 and 2.1 ± 0.2 h at 30 and 50°C, respectively. The hydrolysis activity of the enzyme predominated when the initial lactose concentration used was 5% (w/v). When initial lactose concentration was increased to 20% (w/v), maximum GOS yield obtained was 10% (w/w) achieved at 86% lactose conversion. Analysis using high performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) revealed that the major oligosaccharides produced by the enzyme were 3’-galactosylglucose, 3’-galactosyllactose, 3’-galactobiose, and allolactose, thus showing that this enzyme would prefer to form β-(13)- and β-(16)-linked GOS. Despite its predominantly hydrolytic activity, Saphera synthesised prebiotic GOS which could be interesting to dairy industry.

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Characterization and Application of a New β-Galactosidase Gal42 From Marine Bacterium Bacillus sp. BY02

Cited by 8 publications

References 36 publications

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Evaluation of transgalactosylation activity of commercial β-galactosidase from Bifidobacterium bifidum for synthesis of prebiotic oligosaccharides

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