Kato Y, Matsushita J, Kubodera T, Matsuda K
J Biochem. 1985 Mar;97(3):801-10. doi: 10.1093/oxfordjournals.jbchem.a135120.
An enzyme producing isoprimeverose from xyloglucan fragment oligosaccharides has been purified to the electrophoretically pure state from a commercial enzyme preparation of Aspergillus oryzae (Sanzyme 1000). The purified enzyme showed approximately 1,280-fold increase of the specific activity over the original preparation. The purified enzyme was shown to be an oligomeric protein consisting of two subunits, each of which had a molecular weight of 115,000. The enzyme showed the highest activity at pH 5.0 and 60 degrees C, and was stable in the pH range from 5 to 7 and at up to 50 degrees C. The isoelectric point of this enzyme was pH 3.9. The purified enzyme was highly specific for xyloglucan fragment oligosaccharides and split off isoprimeverose units from the non-reducing end of the backbone of the substrate.
一种能从木葡聚糖片段寡糖产生异麦芽糖的酶已从米曲霉的商业酶制剂(Sanzyme 1000)中纯化至电泳纯状态。纯化后的酶比原始制剂的比活性提高了约1280倍。纯化后的酶是一种由两个亚基组成的寡聚蛋白,每个亚基的分子量为115,000。该酶在pH 5.0和60℃时表现出最高活性,在pH 5至7的范围内以及高达50℃时稳定。这种酶的等电点为pH 3.9。纯化后的酶对木葡聚糖片段寡糖具有高度特异性,并从底物主链的非还原端切下异麦芽糖单位。