A novel bgl1 gene, encoding GH3 family β-glucosidase from Penicillium verruculosum (PvBGL), was cloned and heterologously expressed in P. canescens RN3-11-7 (niaD-) strain under the control of the strong xylA gene promoter. The recombinant rPvBGL was purified and their properties were studied in comparison with those of rAnBGL from Aspergillus niger expressed previously in the same fungal host. The rPvBGL had an observed molecular mass of 90 kDa (SDS-PAGE data) and displayed the enzyme maximum activity at pH 4.6 and 65 °C. The enzyme half-life time at 60 °C was found to be 87 min. Unlike the rAnBGL, the rPvBGL was not adsorbed on microcrystalline cellulose, which gives the latter enzyme an advantage in cellulose conversion with a longer time of hydrolysis.

中文翻译：

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绿青霉的重组GH3家族β-葡萄糖苷酶的克隆，纯化及研究。

在强大的xylA基因启动子的控制下，克隆了一个编码来自vericulium v​​erruculosum（PvBGL）的GH3家族β-葡萄糖苷酶（bvlGL）的新型bgl1基因，并在该菌株中进行了异源表达。纯化了重组rPvBGL，并与先前在同一真菌宿主中表达的黑曲霉rAnBGL的性质进行了比较。rPvBGL的分子量为90 kDa（SDS-PAGE数据），在pH 4.6和65°C下显示酶的最大活性。发现在60℃的酶半衰期为87分钟。与rAnBGL不同，rPvBGL没有吸附在微晶纤维素上，这使后者酶在纤维素转化中具有优势，具有更长的水解时间。