首页> 外文期刊>International Journal of Molecular Sciences >Production of Galactooligosaccharides Using β-Galactosidase Immobilized on Chitosan-Coated Magnetic Nanoparticles with Tris(hydroxymethyl)phosphine as an Optional Coupling Agent
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Production of Galactooligosaccharides Using β-Galactosidase Immobilized on Chitosan-Coated Magnetic Nanoparticles with Tris(hydroxymethyl)phosphine as an Optional Coupling Agent

机译:使用固定在壳聚糖包被的磁性纳米粒子上的β-半乳糖苷酶制备三聚半乳糖,以三(羟甲基)膦为偶联剂。

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β-Galactosidase was immobilized on chitosan-coated magnetic Fe3O4 nanoparticles and was used to produce galactooligosaccharides (GOS) from lactose. Immobilized enzyme was prepared with or without the coupling agent, tris(hydroxymethyl)phosphine (THP). The two immobilized systems and the free enzyme achieved their maximum activity at pH 6.0 with an optimal temperature of 50 °C. The immobilized enzymes showed higher activities at a wider range of temperatures and pH. Furthermore, the immobilized enzyme coupled with THP showed higher thermal stability than that without THP. However, activity retention of batchwise reactions was similar for both immobilized systems. All the three enzyme systems produced GOS compound with similar concentration profiles, with a maximum GOS yield of 50.5% from 36% (w·v−1) lactose on a dry weight basis. The chitosan-coated magnetic Fe3O4 nanoparticles can be regenerated using a desorption/re-adsorption process described in this study.
机译:β-半乳糖苷酶被固定在壳聚糖包被的磁性Fe 3 O 4 纳米颗粒上,用于从乳糖中生产低聚半乳糖(GOS)。在有或没有偶联剂三(羟甲基)膦(THP)的条件下制备固定化酶。两种固定化系统和游离酶均在最适温度为50°C的pH 6.0下达到最大活性。固定化酶在更宽的温度和pH范围内显示出更高的活性。此外,与THP偶联的固定化酶比没有THP的酶具有更高的热稳定性。然而,对于两种固定系统,分批反应的活性保留相似。这三种酶系统均产生了具有相似浓度曲线的GOS化合物,以干重计,36%(w·v -1 )乳糖的最大GOS产率为50.5%。壳聚糖包覆的磁性Fe 3 O 4 纳米颗粒可以使用本研究中描述的解吸/再吸附工艺进行再生。

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