CBM33 蛋白对纤维素的酶切作用。
Cleavage of cellulose by a CBM33 protein.
机构信息
Department of Chemistry Biotechnology and Food Science, Norwegian University of Life Sciences, Aas, Norway.
出版信息
Protein Sci. 2011 Sep;20(9):1479-83. doi: 10.1002/pro.689. Epub 2011 Aug 8.
Abstract
Bacterial proteins categorized as family 33 carbohydrate-binding modules (CBM33) were recently shown to cleave crystalline chitin, using a mechanism that involves hydrolysis and oxidation. We show here that some members of the CBM33 family cleave crystalline cellulose as demonstrated by chromatographic and mass spectrometric analyses of soluble products released from Avicel or filter paper on incubation with CelS2, a CBM33-containing protein from Streptomyces coelicolor A3(2). These enzymes act synergistically with cellulases and may thus become important tools for efficient conversion of lignocellulosic biomass. Fungal proteins classified as glycoside hydrolase family 61 that are known to act synergistically with cellulases are likely to use a similar mechanism.
摘要
最近发现，归类为家族 33 碳水化合物结合模块 (CBM33) 的细菌蛋白可通过水解和氧化作用切割结晶几丁质。我们在这里展示了 CBM33 家族的某些成员可切割结晶纤维素，这可通过 CelS2（来自链霉菌 A3(2)的含有 CBM33 的蛋白）孵育从 Avicel 或滤纸中释放的可溶性产物的色谱和质谱分析证明。这些酶与纤维素酶协同作用，因此可能成为有效转化木质纤维素生物质的重要工具。已知与纤维素酶协同作用的真菌蛋白被归类为糖苷水解酶家族 61，它们可能使用类似的机制。
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