The key Laboratory on Luminescent and Real-Time Analytical Chemistry, Ministry of Education, College of Chemistry and Chemical Engineering, Southwest University, Chongqing, 400715, P. R. China.
College of Life Sciences, Wuhan University, Wuhan, Hubei, 430072, P. R. China.
Sci Rep. 2017 Feb 22;7:43141. doi: 10.1038/srep43141.
Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for the intrinsic peroxidase-like activity of ficin and designed experiments to examine its effectiveness in a variety of scenarios. Ficin can transform peroxidase substrates to colored products in the existence of HO. Our results also indicate that the active sites of peroxidase-like activity of ficin are different from that of protease, which reveals that one enzyme may catalyze more than one kind of substrate to perform different types of reactions. On the basis of these findings, HO releasing from MCF-7 cells was detected successfully. Our findings support a wider application of ficin in biochemistry and open up the possibility of utilizing ficin as enzymatic mimics in biotechnology and environmental monitoring.
木瓜凝乳蛋白酶被归类为一种巯基蛋白酶，从无花果树的乳胶中分离出来。在大多数情况下，一种特定的酶适合几种类型的底物，并催化一种类型的反应。在这项研究中，我们找到了木瓜凝乳蛋白酶固有过氧化物酶样活性的充分证据，并设计实验来检查其在各种情况下的效果。在 HO 的存在下，木瓜凝乳蛋白酶可以将过氧化物酶底物转化为有色产物。我们的结果还表明，木瓜凝乳蛋白酶过氧化物酶样活性的活性位点与蛋白酶的不同，这表明一种酶可以催化不止一种底物来执行不同类型的反应。基于这些发现，成功地检测到 MCF-7 细胞中 HO 的释放。我们的发现支持木瓜凝乳蛋白酶在生物化学中的更广泛应用，并为利用木瓜凝乳蛋白酶作为生物技术和环境监测中的酶模拟物开辟了可能性。
