Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1
Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1
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DOI：
10.1042/bj3240833
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发表时间：
1997-06-15
影响因子：
4.1
通讯作者：
Pettersson, G
中科院分区：
文献类型：
--
作者：
Henriksson, G;Salumets, A;Pettersson, G
比较了黄孢原毛革菌纤维二糖脱氢酶（CDH）和里氏木霉纤维二糖水解酶1（CBH 1）与纤维素的结合等温线。CDH比CBH 1更强地但更稀疏地与纤维素结合。在经典的Scatchard分析中，CDH比CBH 1更适合于单位点结合模型。这两种酶的结合在乙二醇的存在下减少，在硫酸铵的存在下增加，并且不受氯化钠的影响。通过将酶消化的CDH暴露于纤维素并分离纤维素结合的肽，也已经尝试定位CDH上的纤维素结合位点。结果表明，纤维素结合位点位于CDH的氨基酸序列的内部。
The binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been compared with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. CDH binds more strongly but more sparsely to cellulose than does CBH 1. In a classical Scatchard analysis, a better fit to a one-site binding model was obtained for CDH than for CBH 1. The binding of both enzymes decreased in the presence of ethylene glycol, increased in the presence of ammonium sulphate and was unaffected by sodium chloride. Attempts to localize the cellulose-binding site on CDH have also been made by exposing enzymically digested CDH to cellulose and isolating the cellulose-bound peptides. The results suggest that the cellulose-binding site is located internally in the amino acid sequence of CDH.