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Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1
- Henriksson, G (author)
- Salumets, A (author)
-
- Divne, Christina (author)
- KTH,Skolan för bioteknologi (BIO)
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- Pettersson, G (author)
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- (creator_code:org_t)
- Portland Press Ltd. 1997
- 1997
- English.
- In: Biochemical Journal. - : Portland Press Ltd.. - 0264-6021 .- 1470-8728. ; 324, s. 833-838
- Journal article (peer-reviewed)
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- 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.
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