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Hydrolysis of galacto-oligosaccharides in soy molasses by α -galactosidases and invertase from Aspergillus terreus

机译:α-半乳糖苷酶和蔗糖转化酶转化大豆糖蜜中的半乳糖低聚糖

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摘要

Two α -galactosidase (P1 and P2) and one invertase present in the culture of Aspergillus terreus grown on wheat straw for 168 h at 28?oC were partially purified by gel filtration and hydrophobic interaction chromatographies. Optimum pH and temperatures for P1, P2 and invertase preparations were 4.5-5.0, 5.5 and 4.0 and 60, 55 and 65?oC, respectively. The K M app for ?? -nitrophenyl-α -D-galactopyranoside were 1.32 mM and 0.72 mM for P1 and P2, respectively, while the K M app value for invertase, using sacarose as a substrate was 15.66 mM. Enzyme preparations P1 and P2 maintained their activities after pre-incubation for 3 h at 50?oC and invertase maintained about 90% after 6 h at 55 ?oC. P1 and P2 presented different inhibition sensitivities by Ag+, D-galactose, and SDS. All enzyme preparations hydrolyzed galacto-ologosaccharides present in soymolasses.
机译:通过凝胶过滤和疏水相互作用色谱法部分纯化了麦秸中在28℃下生长168 h的曲霉曲霉培养物中存在的两种α-半乳糖苷酶(P1和P2)和一种转化酶。 P1,P2和转化酶制剂的最佳pH和温度分别为4.5-5.0、5.5和4.0以及60、55和65?oC。适用于??的K M应用对于P1和P2,-硝基苯基-α-D-吡喃半乳糖苷分别为1.32mM和0.72mM,而以蔗糖为底物的转化酶的K M app值为15.66mM。酶制剂P1和P2在50°C下预孵育3小时后仍能保持其活性,而在55°C下6小时后转化酶则可保持约90%。 P1和P2对Ag +,D-半乳糖和SDS具有不同的抑制敏感性。所有酶制剂均水解存在于豆浆中的半乳寡糖。

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