Martínez-Morales Fernando, Bertrand Brandt, Pasión Nava Angélica A, Tinoco Raunel, Acosta-Urdapilleta Lourdes, Trejo-Hernández María R
Laboratorio de Biotecnología Ambiental, Centro de Investigación en Biotecnología, Universidad Autónoma del Estado de Morelos, Avenida Universidad 1001, Chamilpa, CP 62209, Cuernavaca, Morelos, Mexico.
Biotechnol Lett. 2015 Feb;37(2):391-6. doi: 10.1007/s10529-014-1679-y. Epub 2014 Sep 26.
Two laccase isoforms (lcc1 and lcc2) produced by Trametes versicolor, grown on oak sawdust under solid-state fermentation conditions, were purified and characterized. The two isoforms showed significant biochemical differences. Lcc1 and lcc2 had MWs of 60 and 100 kDa, respectively. Both isoforms had maximal activity at pH 3 with ABTS and 2,6-dimethyloxyphenol (DMP). Lcc1 was the most attractive isoform due to its greater affinity towards all the laccase substrates used. Lcc1 had Km values of 12, 10, 15 and 17 mM towards ABTS, DMP, guaiacol and syringaldazine, respectively. Lcc2 had equivalent values of 45, 47, 15 and 39 mM. The biochemical properties of lcc1 substantiate the potential of this enzyme for application in the treatment of contaminated water with low pH values and high phenolic content.
对在固态发酵条件下于橡木锯末上生长的云芝所产生的两种漆酶同工型(lcc1和lcc2)进行了纯化和表征。这两种同工型表现出显著的生化差异。Lcc1和lcc2的分子量分别为60 kDa和100 kDa。两种同工型在pH 3时对ABTS和2,6 - 二甲基氧化酚(DMP)具有最大活性。由于Lcc1对所有所使用的漆酶底物具有更高的亲和力,因此它是最具吸引力的同工型。Lcc1对ABTS、DMP、愈创木酚和丁香醛连氮的米氏常数分别为12、10、15和17 mM。Lcc2的相应值为45、47、15和39 mM。Lcc1的生化特性证实了该酶在处理低pH值和高酚含量的受污染水方面的应用潜力。