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- W2024664583 abstract "Two galactanases, purified from experimental enzyme preparations derived from Aspergillus niger and Aspergillus aculeatus were found to be similar in a number of properties. They had similar molecular weights (Mr = 42–43 kD) and both showed highest activity on 1,4-β-D-galactan. Optimal activity was measured at 50–55°C and pH 4·00–4·25; optimal stability was observed in the pH range of 5–7 at 30°C. A sodium acetate buffer was found to be the best incubation buffer. Activity and stability were affected by Pb2+ (endo-galactanase from A. aculeatus was inhibited completely) and to a lesser extent by Ag+ and Zn2+ ions. Digestion of (arabino)-1,4-β-D-galactan resulted initially in a big shift in the Mw value of the bulk of (arabino)-1,4-β-D-galactan and formation of low galacto-oligomers, mainly tetra- and trimers of galactose. In the final stage of the reaction mono- and dimer accumulated as end products. Therefore a multiple attack mechanism was suggested for the endo-1,4-β-D-galactanases. The galactanases did not hydrolyse arabino-1,3/6-β-D-galactan. The effect of the temperature on their stability, their specific activities and their affinity for potato arabinogalactan differed; in the absence of substrate the A. niger and A. aculeatus endo-galactanase were stable up to 60°C and 35°C, respectively. The specific activities on potato arabinogalactan in a sodium acetate buffer pH 5·0, 30°C were found to be 158 and 244 u/mg, respectively. The Km values estimated for potato arabinogalactan were 0·77 and 0·31 g/litre, respectively. For an optimal breakdown of potato arabinogalactan combined action of arabinanases from A. niger and endo-galactanase was required. Arabinofuranosidase B did not stimulate the degradation of potato arabinogalactan by the endo-galactanases under the conditions used, whereas endo-1,5-α-L-arabinanase had an immediate synergistic effect with both endo-galactanases, indicating the presence of linear 1,5-α-L-arabinan side chains." @default.
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- W2024664583 title "Purification and characterization of Endo-1,4-β-D-galactanases from Aspergillus niger and Aspergillus aculeatus: Use in combination with arabinanases from Aspergillus niger in enzymic conversion of potato arabinogalactan" @default.
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- W2024664583 doi "https://doi.org/10.1016/0144-8617(91)90101-h" @default.
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