A pectinase-producing strain, Lichtheimia sp. X-8, was isolated from the soil for the first time. Subsequently, Lichtheimia sp. UV-16, with a 1.23-fold increase in pectinase activity, was obtained via UV mutagenesis, and optimization of its liquid fermentation process boosted pectinase activity from 455.6 ± 12.7 to 3202.0 ± 82.1 U/mL. The crude enzyme was purified by salting out and anion exchange resin, with a purification ratio of 2.28-fold and a yield of 36.5%. The optimal reaction temperature for the pure enzyme was 60 °C with an optimal pH of 5.5. Thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) confirmed that the enzyme was an exopolygalacturonase, achieving over 99% efficiency in pectin hydrolysis. Furthermore, incorporating pure enzymes into juice pulps can substantially enhance the juice yield, which makes this polygalacturonase a promising application in the beverage industry.

中文翻译：

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新型菌株 Lichtheimia sp. UV-16 的胞外多聚半乳糖醛酸酶生产和酶水解特性


一种产生果胶酶的菌株，Lichtheimia sp.X-8 首次从土壤中分离出来。随后，通过紫外线诱变获得果胶酶活性增加 1.23 倍的 Lichtheimia sp. UV-16，优化其液体发酵过程将果胶酶活性从 455.6 ± 12.7 提高到 3202.0 ± 82.1 U/mL。盐析和阴离子交换树脂纯化粗酶，纯化比例为 2.28 倍，收率为 36.5%。纯酶的最佳反应温度为 60 °C，最适 pH 值为 5.5。薄层色谱 （TLC） 和高效液相色谱 （HPLC） 证实该酶是一种胞外多聚半乳糖醛酸酶，在果胶水解中实现了超过 99% 的效率。此外，将纯酶掺入果汁果肉中可以显著提高果汁产量，这使得这种多聚半乳糖醛酸酶在饮料行业中具有前景。