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• W2027420643 endingPage "532" @default.
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• W2027420643 abstract "An acid β-galactosidase was isolated from the digestive juice of Achatina achatina and purified to homogeneity by anion exchange, gel-filtration and hydroxyapatite chromatographies. This enzyme is soluble, as are the cytosolic β-galactosidases, functions at acid pH like the lysosomal enzymes but differs from the other soluble animal β-galactosidases in that it is highly specific for the β-d-galactosyl residue. In addition, it cleaves the β1–4 linkage much faster than the β1–3 and β1–6 linkages. The enzyme is a monomeric glycoprotein with a molecular mass of 120–125 kDa and the carbohydrate moiety makes up approximately 6% (w/w) of the protein. The amino acid composition displays an important amount of acidic/amide and hydroxy amino acid residues and a low content of basic residues. The enzyme activity is markedly affected by the ionic strength of the medium and the rate–pH curve was shifted towards higher pH values in the presence of added salt. Acid β-galactosidase is capable of catalysing transgalactosylation reactions. The yields of galactosylation of hydroxy amino acid derivatives, catalysed by the enzyme in the presence of lactose as the glycosyl donor, were higher than those reported previously with conventional sources of β-galactosidases. In addition, the pH optimum is different for the hydrolysis (pH 3.2) and transgalactosylation (pH 5.0) reactions. On the basis of this work, the enzyme could be used as a tool in the structural analysis of d-galactose-containing oligosaccharide chains, as well as for the synthesis of glycoconjugates." @default.
• W2027420643 created "2016-06-24" @default.
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• W2027420643 date "1997-10-01" @default.
• W2027420643 modified "2023-10-16" @default.
• W2027420643 title "Characterization of a strictly specific acid β-galactosidase from Achatina achatina" @default.
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• W2027420643 doi "https://doi.org/10.1016/s0304-4165(97)00065-2" @default.
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