Ricklefs Esther, Winkler Nadine, Koschorreck Katja, Urlacher Vlada B
Institute of Biochemistry, Heinrich-Heine University Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany.
Institute of Biochemistry, Heinrich-Heine University Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany.
J Biotechnol. 2014 Dec 10;191:46-53. doi: 10.1016/j.jbiotec.2014.05.031. Epub 2014 Jun 6.
Laccases are oxidases with potential for application in biotechnology. Up to now only fungal laccases have been applied in technical processes, although bacterial laccases are generally easier to handle and more stable at alkaline pH values and elevated temperatures. To increase the toolbox of bacterial laccases and to broaden our knowledge about them, new enzymes have to be characterized. Within this study, we describe the new bacterial laccase CgL1 from Corynebacterium glutamicum. CgL1 was found to oxidize typical laccase substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid), syringaldazine and 2,6-dimethoxyphenol. The enzyme also demonstrates cuprous oxidase activity. Furthermore, CgL1 is active for several hours at temperatures up to 60°C and at alkaline pH, as well as stable in different organic solvents. This makes CgL1 a potential candidate for technical applications. In addition, CgL1 was found to catalyze the CC/CO coupling of several phenolic compounds which can serve as precursors for the synthesis of natural products like antibiotics and phytohormones. This activity and product distribution were influenced by pH value and mediators used.
漆酶是一种氧化酶，在生物技术领域具有应用潜力。到目前为止，尽管细菌漆酶通常更易于操作，并且在碱性pH值和较高温度下更稳定，但只有真菌漆酶被应用于工业生产过程。为了增加细菌漆酶的种类，并拓宽我们对它们的了解，必须对新的酶进行表征。在本研究中，我们描述了来自谷氨酸棒杆菌的新型细菌漆酶CgL1。发现CgL1能够氧化典型的漆酶底物，如2,2'-联氮双(3-乙基苯并噻唑啉-6-磺酸)、丁香醛连氮和2,6-二甲氧基苯酚。该酶还具有氧化亚铜酶活性。此外，CgL1在高达60°C的温度和碱性pH条件下能保持活性数小时，并且在不同的有机溶剂中也很稳定。这使得CgL1成为工业应用的潜在候选酶。此外，发现CgL1能催化几种酚类化合物的碳-碳/碳-氧偶联反应，这些酚类化合物可作为合成抗生素和植物激素等天然产物的前体。这种活性和产物分布受pH值和所用介质的影响。
