Gerardi C, Blando F, Santino A, Zacheo G
Istituto di Ricerca sulle Biotecnologie Agroalimentari, CNR, Via Prov.le Lecce-Monteroni, 73100, Lecce, Italy
Plant Sci. 2001 Apr;160(5):795-805. doi: 10.1016/s0168-9452(00)00423-4.
A beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) was purified to homogeneity from ripe fruits of sweet cherry (Prunus avium L.) by ammonium sulphate precipitation, ion exchange and size exclusion chromatography. The enzyme is a monomer with a molecular mass of approximately 68 kDa and an acidic isoelectric point. N-terminal sequence analysis indicated that sweet cherry beta-glucosidase is related to other plant cyanogenic beta-glucosidases. Substrate specificity studies revealed that the enzyme is able to attack and hydrolyse several synthetic substrates and total cell walls purified from ripe fruit. Biochemical and immunolocalisation studies showed that sweet cherry beta-glucosidases are mainly localised in the cytosol and in the apoplast, at the unripe stage of ripening; in ripe fruit it is also associated with cell wall.
通过硫酸铵沉淀、离子交换和尺寸排阻色谱法，从甜樱桃（Prunus avium L.）成熟果实中纯化出一种β-葡萄糖苷酶（β-D-葡萄糖苷葡糖水解酶，EC 3.2.1.21），使其达到同质。该酶是一种单体，分子量约为68 kDa，具有酸性等电点。N端序列分析表明，甜樱桃β-葡萄糖苷酶与其他植物生氰β-葡萄糖苷酶相关。底物特异性研究表明，该酶能够作用并水解几种合成底物以及从成熟果实中纯化的总细胞壁。生化和免疫定位研究表明，甜樱桃β-葡萄糖苷酶在果实成熟的未成熟阶段主要定位于细胞质和质外体；在成熟果实中，它也与细胞壁相关。
