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Partial purification and characterization of polygalacturonase-inhibitor proteins from pearl millet

机译:珍珠粟中半乳糖醛酸酶抑制剂蛋白的部分纯化和表征

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Polygalacturonase-inhibitor proteins (PGIPs) are plant cell wall glycoproteins, involved in the inhibition of microbial endo-polygalacturonases (EPGs). The present study involved activity guided partial purification of pearl millet?[Pennisetum glaucum?(L.) R.Br.]?protein extract by cation exchange chromatography, which resulted in two pooled protein peaks – Peak-A and Peak-B, both of which showed inhibitory activity against the?Aspergillus niger?EPG. Protein separation of the two peaks by gel electrophoresis showed prominent bands between 29 and 43 kDa, consistent with the molecular weights of the known plant PGIPs. The two PGIP peaks were further studied for their inhibitory activities with respect to three parameters viz., inhibitor concentration, pH and temperature effects. Enzyme inhibition was partial and increased with inhibitor concentration. The Peak-B was found to be the more active inhibitor of the two. The results indicate the presence of at least two isoforms of PGIP in pearl millet. This is the first such study to be undertaken in understanding the presence of the PGIPs in millets.
机译:聚半乳糖醛酸酶抑制剂蛋白(PGIP)是植物细胞壁糖蛋白,参与抑制微生物内聚半乳糖醛酸酶(EPG)。本研究涉及通过阳离子交换色谱法对珍珠mill?[Pennisetum glaucum?(L.R.Br。)?]蛋白提取物进行活性导向的部分纯化,产生了两个合并的蛋白峰-Peak-A和Peak-B,两者其中显示出对黑曲霉EPG的抑制活性。通过凝胶电泳分离的两个峰的蛋白质显示出29 kDa和43 kDa之间的显着条带,与已知植物PGIP的分子量一致。就三个参数,即抑制剂浓度,pH和温度影响,进一步研究了两个PGIP峰的抑制活性。酶抑制是部分的,并随着抑制剂浓度的增加而增加。发现Peak-B是两者中更有效的抑制剂。结果表明在珍珠小米中存在至少两种PGIP同工型。这是第一个了解小米中PGIP的存在的研究。

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