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首页> 外文期刊>Catalysis Letters >Functional Characterization of a New Cold-Adapted β-Galactosidase from an Arctic Fjord Sediment Bacteria Enterobacter ludwigii MCC 3423
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Functional Characterization of a New Cold-Adapted β-Galactosidase from an Arctic Fjord Sediment Bacteria Enterobacter ludwigii MCC 3423

机译：来自北极峡湾沉积物细菌的新冷适应β-半乳糖苷酶的功能表征<重点型=“斜体”>肠杆菌Ludwigii MCC 3423

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摘要

In the present study, a new cold-adapted β-galactosidase, BgalEL isolated from the fjord sediment bacteria, Enterobacter ludwigii MCC 3423, was purified and characterized. The phylogenetic analysis of partial sequence of bgalEL gene revealed 99% relatedness of the enzyme to Enterobacter cloacae β-galactosidase. BgalEL is a homotetramer with molecular weight 465?kDa composed of ~?116.42?kDa subunits. The optimal pH range and temperature for maximum hydrolytic activity on ONPG were 7.0–8.0 and 45?°C respectively. BgalEL was stable at pH ranges 6.0–8.0. The K m and V max for BgalEL were recorded as 2.03?mM and 49.3?U?mg_(?1)respectively. The product formation by BgalEL was modelled with various degradation kinetic models and zeroth was found as model was best-fitted model. The kinetic half-life period of ONPG was noted as 9.0?×?10_(?4). The presence of K_(+), Mg_(2+)and Mn_(2+)at 10?mM concentrations stimulated BgalEL activity by 31?±?3.9, 34?±?1.2 and 42?±?1.9% respectively. It was interesting to see that BgalEL was least affected by the hydrolytic products, glucose and galactose. Noteworthy, effect of Ca_(2+)ions on BgalEL activity was negligible at concentrations of 10?mM. BgalEL hydrolyzed lactose in milk at refrigerated temperature and also displayed transglycosylation potential in the presence of substantial concentrations of lactose at 40?°C. Finally, this is the first report with such a detailed characterization of β-galactosidase enzyme from a gram-negative bacterium isolated from the Arctic region. In light of the above mentioned properties, we thus recommend the enzyme BgalEL for the large scale production lactose free milk for the safe consumption in lactose-intolerance and the prebiotic galactooligosaccharides as supplement for infant food formulas. Graphical Abstract.
机译：在本研究中，纯化并表征了一种新的一种新的冷适应的β-半乳糖苷酶，从峡湾沉积物细菌中分离的BGalel，肠杆菌沉积物细菌。 BGalel基因部分序列的系统发育分析显示酶与肠杆菌β-半乳糖苷酶的99％相关性。 Bgalel是一个具有分子量465？KDA组成的同源体，由〜〜116.42？KDA亚基组成。 ONPG上最大水解活性的最佳pH范围和温度分别为7.0-8.0和45°C。 Bgalel在pH值范围内稳定6.0-8.0。 Bgalel的K M和V Max分别记录为2.03Ωmm和49.3？u？mg _（？1）。 Bgalel的产物形成用各种降解动力学模型进行建模，并发现Zeroth作为模型是最适合的模型。 ONPG的动力学半衰期被指出为9.0？×10 _（？4）。在10μmmm浓度下的K _（+），Mg_（2+）和Mn_（2+）的存在刺激Bgalel活性31°±3.9,34？±1.2和42？±1.9％。有趣的是，BGALEL受水解产物，葡萄糖和半乳糖的影响最小。值得注意的是，Ca_（2+）离子对Bgalel活性的影响浓度可忽略10？mm。在冷藏温度下牛奶中的Bgalel水解乳糖，并且在40℃下存在在大量乳糖的情况下显示出常糖基化电位。最后，这是第一报告，其具有来自从北极区域分离的革兰阴性细菌的β-半乳糖苷酶的这种详细表征。根据上述性质，我们推荐为大规模生产乳糖游离牛奶的酶Bgalel用于乳糖 - 不耐受和益生元脱寡聚糖作为婴儿食品公式的补充剂。图形概要。

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