A polygalacturonase with a molecular mass of 74 kDa, an isoelectric point around pH 4.2 and pH--and temperature optima of 3.9 and 50 degrees C, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-alpha-1,4-polygalacturonase (exo-PG I). Km and Vmax for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U x mg(-1), respectively. The enzyme, a glycoprotein with a carbohydrate content of 81%, is probably the main pectinase of Penicillium frequentans responsible for cleaving monomer units from the non-reducing end of pectin.

中文翻译：

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频繁青霉中胞外半乳糖醛酸酶I的纯化和部分表征。

从青霉菌的培养液中纯化了分子量为74 kDa，等电点约为pH 4.2和pH的最佳半乳糖苷酸酶，以及最适温度分别为3.9和50摄氏度。将该酶表征为外切α-1，4-聚半乳糖醛酸酶（exo-PG I）。多果酸钠水解的Km和Vmax分别为0.68 g / l和596.8 U x mg（-1）。该酶是一种糖蛋白，其碳水化合物含量为81％，可能是青霉的主要果胶酶，负责从果胶的非还原端裂解单体单元。