Evaluation of the Potential of Fungal and Plant Laccases for Active-Packaging Applications
Evaluation of the Potential of Fungal and Plant Laccases for Active-Packaging Applications
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DOI：
10.1021/jf103811g
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发表时间：
2011-05-25
影响因子：
6.1
通讯作者：
Jonsson, Leif J.
中科院分区：
文献类型：
--
作者：
Chatterjee, Robin;Johansson, Kristin;Jonsson, Leif J.
研究了来自变色栓菌 (TvL)、嗜热毁丝霉 (MtL) 和漆树 (RvL) 的漆酶在含有易发生氧化反应的食品的活性包装中作为氧清除剂的潜在用途。使用一组 17 种还原底物（主要是酚类化合物）研究了漆酶的底物选择性。研究了在低温（4-31 摄氏度）下进行的反应的温度依赖性。此外，将漆酶固定在乳胶/粘土基质中，并在高达 105°C 的温度下进行干燥程序。结果表明，在分散体包被、75-105°C 干燥以及随后在 4°C 下储存含酶膜后，可以固定保留活性的漆酶。TvL 和在某种程度上 MtL 就其还原底物而言是混杂的，从某种意义上说，所测试的 17 种底物的活性相对较小。另一方面，RvL 显示出高选择性，主要针对类似于其天然底物漆酚的底物。在 7 摄氏度下进行测试时，所有三种漆酶均保留了其在 25 摄氏度下的活性的 20% 以上，这表明漆酶也可以在冷藏食品包装中使用。包衣和干燥导致剩余酶活性在 18% 至 53% 之间，具体取决于所使用的干燥条件。结果表明，漆酶可用于活性包装应用，并且还原底物的选择性是不同来源漆酶的重要特征。
Laccases from Trametes versicolor (TvL), Myceliophthora thermophila (MtL), and Rhus vernicifera (RvL) were investigated with regard to their potential utilization as oxygen scavengers in active packages containing food susceptible to oxidation reactions. The substrate selectivity of the laccases was investigated with a set of 17 reducing substrates, mainly phenolic compounds. The temperature dependence of reactions performed at low temperatures (4-31 degrees C) was studied. Furthermore, the laccases were subjected to immobilization in a latex/clay matrix and drying procedures performed at temperatures up to 105 degrees C. The results show that it is possible to immobilize the laccases with retained activity after dispersion coating, drying at 75-105 degrees C, and subsequent storage of the enzyme-containing films at 4 degrees C. TvL and, to some extent, MtL were promiscuous with regard to their reducing substrate, in the sense that the difference in activity with the 17 substrates tested was relatively small. RvL, on the other hand, showed high selectivity, primarily toward substrates resembling its natural substrate urushiol. When tested at 7 degrees C, all three laccases retained > 20% of the: activity they had at 25 degrees C, which suggests that it would be possible to utilize the laccases also in refrigerated food packages. Coating and drying resulted in a remaining enzymatic activity ranging from 18 to 53%, depending on the drying conditions used. The results indicate that laccases are useful for active-packaging applications and that the selectivity for reducing substrates is an important characteristic of laccases from different sources.