Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Post Office Box 5003, 1432 Ås, Norway.
Science. 2010 Oct 8;330(6001):219-22. doi: 10.1126/science.1192231.
Efficient enzymatic conversion of crystalline polysaccharides is crucial for an economically and environmentally sustainable bioeconomy but remains unfavorably inefficient. We describe an enzyme that acts on the surface of crystalline chitin, where it introduces chain breaks and generates oxidized chain ends, thus promoting further degradation by chitinases. This enzymatic activity was discovered and further characterized by using mass spectrometry and chromatographic separation methods to detect oxidized products generated in the absence or presence of H(2)(18)O or (18)O(2). There are strong indications that similar enzymes exist that work on cellulose. Our findings not only demonstrate the existence of a hitherto unknown enzyme activity but also provide new avenues toward more efficient enzymatic conversion of biomass.
高效的酶促转化对于经济和环境可持续的生物经济至关重要，但目前效率并不理想。我们描述了一种作用于晶体几丁质表面的酶，它在晶体几丁质表面引入链断裂，并产生氧化的链末端，从而促进几丁质酶进一步降解。这种酶促活性是通过使用质谱和色谱分离方法来检测在没有或存在 H(2)(18)O 或 (18)O(2)的情况下生成的氧化产物而发现和进一步表征的。有强有力的迹象表明，类似的作用于纤维素的酶也存在。我们的发现不仅证明了一种迄今未知的酶活性的存在，而且为更有效地酶促转化生物质提供了新的途径。
