Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates
Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates
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DOI：
10.1016/j.biortech.2010.07.120
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发表时间：
2011-01-01
影响因子：
11.4
通讯作者：
Siika-aho, Matti
中科院分区：
文献类型：
--
作者：
Varnai, Aniko;Viikari, Liisa;Siika-aho, Matti
研究了纯化后的里塞木霉纤维素酶（TrCel7A、TrCel6A和TrCel5A）、木聚糖酶TrXyn11和黑曲霉β -葡萄糖苷酶AnCel3A在两种预处理木质纤维素材料、蒸汽预处理和催化去木素化云杉以及微晶纤维素（Avicel）水解过程中的吸附作用。酶混合物被编译成类似于商业纤维素酶制剂的组成。水解在35℃下进行，以模拟同时糖化和发酵（SSF）的温度。酶吸附后，分析水解上清液中单个游离酶的活性和蛋白量。大多数酶在水解的早期阶段迅速吸附，并在整个水解过程中保持结合，尽管转化率相当高。只有在催化氧化的云杉样品中，当水解度达到80%时，结合酶才开始释放。酶活和蛋白测定结果吻合较好。(C) 2010 Elsevier Ltd.版权所有。
The adsorption of purified Trichoderma reesei cellulases (TrCel7A, TrCel6A and TrCel5A) and xylanase TrXyn11 and Aspergillus niger beta-glucosidase AnCel3A was studied in enzyme mixture during hydrolysis of two pretreated lignocellulosic materials, steam pretreated and catalytically delignified spruce, along with microcrystalline cellulose (Avicel). The enzyme mixture was compiled to resemble the composition of commercial cellulase preparations. The hydrolysis was carried out at 35 degrees C to mimic the temperature of the simultaneous saccharification and fermentation (SSF). Enzyme adsorption was followed by analyzing the activity and the protein amount of the individual free enzymes in the hydrolysis supernatant. Most enzymes adsorbed quickly at early stages of the hydrolysis and remained bound throughout the hydrolysis, although the conversion reached was fairly high. Only with the catalytically oxidized spruce samples, the bound enzymes started to be released as the hydrolysis degree reached 80%. The results based on enzyme activities and protein assay were in good accordance. (C) 2010 Elsevier Ltd. All rights reserved.