Werries E, Nebinger P
Mol Biochem Parasitol. 1984 Apr;11:329-36. doi: 10.1016/0166-6851(84)90076-8.
A beta-amylase like activity isolated from a cell homogenate of Entamoeba histolytica, and separated from other glucohydrolytic activities by gel filtration and isoelectric focusing, hydrolyzed amylose, amylopectin and glycogen, yielding maltose as reaction product. From the non-reducing ends of the 4-nitrophenyl-alpha-D-glycosides of maltotriose, maltotetraose, maltopentaose and maltohexaose the enzyme removed maltose units. The pH optimum for hydrolyzing the poly- and oligosaccharides was pH 6.5, and the temperature optimum was 29 degrees C. Estimation of relative molecular mass by gel filtration on Sephadex G 75 gave values around Mr = 32 000. The isoelectric point was found to be 5.7.
从溶组织内阿米巴细胞匀浆中分离出一种类似β-淀粉酶的活性物质，通过凝胶过滤和等电聚焦将其与其他糖水解活性物质分离。该活性物质能水解直链淀粉、支链淀粉和糖原，生成麦芽糖作为反应产物。它能从麦芽三糖、麦芽四糖、麦芽五糖和麦芽六糖的对硝基苯基-α-D-糖苷的非还原端去除麦芽糖单元。水解多糖和寡糖的最适pH为6.5，最适温度为29℃。在Sephadex G 75上进行凝胶过滤估算相对分子质量，得到的值约为Mr = 32000。发现其等电点为5.7。
