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  • Title: Cloning, Expression, Purification and Characterization of the β-galactosidase PoβGal35A from Penicillium oxalicum.
    Author: Zhou A, Yi H, Yan X, Mao Z, Deng Y, Lv X, Wang D, Zhang X.
    Journal: Mol Biotechnol; 2023 Jul; 65(7):1140-1150. PubMed ID: 36454534.
    Abstract:
    Galactosidases are industrially important enzymes that hydrolyze galactosidic bonds in carbohydrates. Identifying new galactosidases with distinct functional characteristics is of paramount importance. In this study, we report the finding of a novel β-galactosidase PoβGal35A from the fungus Penicillium oxalicum. PoβGal35A belongs to the glycoside hydrolase family 35 (GH35), functions optimally at 70 °C and pH 5.0, and exhibits a specific high activity (191 ± 6.2 U/mg) towards pNPβgal. Ca2+, Fe3+and Ba2+ ions enhance the activity of the enzyme, whereas Cu2+ and Hg2+ significantly reduce it. This enzyme releases galactose from β-1,3-galactan, β-1,4-galactan, β-1,6-galactan, as well as arabinogalactan from larchwood (LWAG). In addition, PoβGal35A acts synergistically with arabinosidase to degrade LWAG. These results suggest that PoβGal35A is a high activity exo-β-1,3/4/6-galactanase that can be used to establish glycan blocks in glycoconjugates, and thus provides a new tool for biotechnological applications.
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