The Michaelis constants ratio for two substrates with a series of fungal (mould and yeast) β-galactosidases

Samoshina, Nataliya M.; Samoshin, Vyacheslav V.

doi:10.1016/j.enzmictec.2004.07.011

Cited by 14 publications

(5 citation statements)

References 114 publications

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“…This finding is in contrast to previously reported results [25,26]. It is easy to understand that b-Gal was synthesized by the host to digest lactose; therefore, the geometry of its active site has high affinity to lactose.…”

Section: Discussioncontrasting

confidence: 85%

Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3

Fan

Xiao

Zhang

et al. 2015

Protein Expression and Purification

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Section: Discussioncontrasting

confidence: 85%

Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3

Fan

Xiao

Zhang

et al. 2015

Protein Expression and Purification

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“…Kinetic constants were determined for the two substrates lactose and oNPG. In accordance with β-galactosidases from a number of different sources (32), the Michaelis constants are significantly lower for the chromogenic model substrate oNPG than for the natural substrate lactose. The kinetic parameters of L103 β-galactosidase with respect to oNPG were not determined due to the similarity of both enzymes, L461 and L103, but it can be expected that the K m,oNPG is also significantly lower than the K m value determined for lactose.…”

Section: Discussionmentioning

confidence: 58%

Purification and Characterization of Two Novel β-Galactosidases from Lactobacillus reuteri

Nguyễn

Splechtna

Steinböck

et al. 2006

J. Agric. Food Chem.

130

151

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The intracellular beta-galactosidase (beta-gal) enzymes from two strains of Lactobacillus reuteri, L103 and L461, were purified by ammonium sulfate fractionation, hydrophobic interaction, and affinity chromatography. Both enzymes are heterodimers with a molecular mass of 105 kDa, consisting of a 35 kDa subunit and a 72 kDa subunit. Active staining of L. reuteri L103 and L461 beta-gal with 4-methylumbelliferyl beta-d-galactoside showed that the intact enzymes as well as the larger subunits possess beta-galactosidase activity. The isoelectric points of L. reuteri L461 and L103 beta-gal were found to be in the range of 3.8-4.0 and 4.6-4.8, respectively. Both enzymes are most active in the pH range of 6-8; however, they are not stable at pH 8. The L. reuteri beta-galactosidases are activated by various mono- and divalent cations, including Na(+), K(+), and Mn(2+), and are moderately inhibited by their reaction products d-glucose and d-galactose. Because of their origin from beneficial and potentially probiotic lactobacilli, these enzymes could be of interest for the synthesis of prebiotic galacto-oligosaccharides.

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“…K m values of the immobilized and the free enzymes were calculated as 0.10 and 0.066, respectively. Generally, K m value increases with the increased amount of the immobilized enzyme . Vmax values were calculated as 0.178 and 0.208 mg/mL for immobilized and free enzymes, respectively.…”

Section: Resultsmentioning

confidence: 99%

Preparation of a Poly(ethylene glycol)‐Based Cross‐Linked Network from a Click Reaction for Enzyme Immobilization

2019

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In this study, a polyethylene glycol (PEG)‐maleimide film was prepared by a thiol‐ene click reaction. The covalent immobilization of amylase was carried out onto the PEG‐maleimide based photo‐curable network via epoxy and C=O groups without any linker. The epoxy and carbonyl groups on the PEG backbone improved the affinity of the enzyme. The immobilization yield of amylase onto the film was 72.46%. The immobilization capacity was also determined as 313 mg/g. The thermal stability of amylase improved via covalent attachment. Immobilized amylase showed maximum activity at 40 °C and pH 6.5. The immobilized amylase continued to retain 66% of its initial activity after 30 days.

show abstract

The Michaelis constants ratio for two substrates with a series of fungal (mould and yeast) β-galactosidases

Cited by 14 publications

References 114 publications

Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3

Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3

Purification and Characterization of Two Novel β-Galactosidases from Lactobacillus reuteri

Preparation of a Poly(ethylene glycol)‐Based Cross‐Linked Network from a Click Reaction for Enzyme Immobilization

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