β-Glucosidase (BGL) is a rate-limiting enzyme of lignocellulose hydrolysis for second-generation bioethanol production, but its inhibition by lignocellulose pretreatment products, ethanol, and salt is apparent. Here, the recombinant Penicillium oxalicum 16 BGL 1 (rPO16BGL1) from Pichia pastoris GS115 kept complete activity at 0.2-1.4 mg/mL furan derivatives and phenolic compounds, 50 mg/mL sodium chloride (potassium chloride), or 100 mg/mL ethanol at 40 °C. rPO16BGL1 retained above 50% residual activity at 30 mg/mL organic acid sodium, and 60% residual activity at 40 °C with 300 mg/mL ethanol. Sodium chloride and potassium chloride had a complicated effect on rPO16BGL1, which resulted in activation or inhibition. The inhibition kinetics of the enzyme reaction demonstrated that organic acids and organic acid sodium were non-competitive inhibitors and that ethanol was a competitive inhibitor at < 1.5 mg/mL salicin. Moreover, substrate inhibition of the enzyme was found at > 2 mg/mL salicin, and the Km/KI and Km/KSI average values revealed that the inhibitory strength was ranked as salicin-organic acids > organic acids > salicin-organic acid sodium salt > organic acid sodium salt > salicin > salicin-KCl > salicin-NaCl > salicin-ethanol > ethanol.

中文翻译：

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重组草酸青霉 16 β-葡萄糖苷酶 1 对多种木质纤维素预处理产品、乙醇和盐表现出全面的抑制抗性。

β-葡萄糖苷酶（BGL）是第二代生物乙醇生产中木质纤维素水解的限速酶，但其受到木质纤维素预处理产物、乙醇和盐的抑制作用是明显的。此处，来自毕赤酵母 GS115 的重组草酸青霉 16 BGL 1 (rPO16BGL1) 在 0.2-1.4 mg/mL 呋喃衍生物和酚类化合物、50 mg/mL 氯化钠（氯化钾）或 100 mg/mL 乙醇（100 mg/mL）条件下保持完全活性。 40°C。rPO16BGL1 在 30 mg/mL 有机酸钠下保留了 50% 以上的残余活性，在 40 °C 使用 300 mg/mL 乙醇时保留了 60% 的残余活性。氯化钠和氯化钾对rPO16BGL1具有复杂的作用，导致激活或抑制。酶反应的抑制动力学表明，有机酸和有机酸钠是非竞争性抑制剂，而乙醇在< 1.5 mg/mL水杨苷时是竞争性抑制剂。此外，在> 2 mg/mL水杨苷时发现该酶的底物抑制，并且Km/KI和Km/KSI平均值显示抑制强度排序为水杨苷-有机酸>有机酸>水杨苷-有机酸钠盐> 有机酸钠盐 > 水杨苷 > 水杨苷-KCl > 水杨苷-NaCl > 水杨苷-乙醇 > 乙醇。