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Isotherms for adsorption of cellobiohydrolase I and II from Trichoderma reesei on microcrystalline cellulose

Medve, J; Ståhlberg, J and Tjerneld, Folke LU (1997) In Applied Biochemistry and Biotechnology 66(1). p.39-56
Abstract
Adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I and II (CBH I and CBH II) from Trichoderma reesei has been studied. Adsorption isotherms of the enzymes were measured at 4 degrees C using CBH I and CBH II alone and in reconstituted equimolar mixtures. Several models (Langmuir, Freundlich, Temkin, Jovanovic) were tested to describe the experimental adsorption isotherms. The isotherms did not follow the basic (one site) Langmuir equation that has often been used to describe adsorption isotherms of cellulases; correlation coefficients (R-2) were only 0.926 and 0.947, for CBH I and II, respectively. The experimental isotherms were best described by a model of Langmuir type with two adsorption sites and by a... (More)
Adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I and II (CBH I and CBH II) from Trichoderma reesei has been studied. Adsorption isotherms of the enzymes were measured at 4 degrees C using CBH I and CBH II alone and in reconstituted equimolar mixtures. Several models (Langmuir, Freundlich, Temkin, Jovanovic) were tested to describe the experimental adsorption isotherms. The isotherms did not follow the basic (one site) Langmuir equation that has often been used to describe adsorption isotherms of cellulases; correlation coefficients (R-2) were only 0.926 and 0.947, for CBH I and II, respectively. The experimental isotherms were best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation); using these models the correlation coefficients were in most cases higher than 0.995. Apparent binding parameters derived from the two sites Langmuir model indicated stronger binding of CBH II compared to CBH I; the distribution coefficients were 20.7 and 3.7 L/g for the two enzymes, respectively. The binding capacity, on the other hand, was higher for CBH I, 1.0 mu mol (67 mg) per gram Avicel, compared to 0.57 mu mol/g (30 mg/g) for CBH II. The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules. (Less)
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Contribution to journal
publication status
published
subject
keywords
SYNERGISM, COMPONENTS, CELLULASES, ENZYMATIC-HYDROLYSIS, LIQUID-CHROMATOGRAPHIC SORBENTS, 2 CELLOBIOHYDROLASES, DOMAIN, VIRIDE, EQUILIBRIA, PROTEINS
in
Applied Biochemistry and Biotechnology
volume
66
issue
1
pages
39 - 56
publisher
Humana Press
external identifiers
  • scopus:0031111375
ISSN
1559-0291
DOI
10.1007/BF02788806
language
English
LU publication?
yes
id
fa8dea2d-c50b-4a58-b9c0-25b04802431b (old id 126194)
date added to LUP
2007-07-06 11:45:19
date last changed
2017-07-30 03:48:43
@article{fa8dea2d-c50b-4a58-b9c0-25b04802431b,
  abstract     = {Adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I and II (CBH I and CBH II) from Trichoderma reesei has been studied. Adsorption isotherms of the enzymes were measured at 4 degrees C using CBH I and CBH II alone and in reconstituted equimolar mixtures. Several models (Langmuir, Freundlich, Temkin, Jovanovic) were tested to describe the experimental adsorption isotherms. The isotherms did not follow the basic (one site) Langmuir equation that has often been used to describe adsorption isotherms of cellulases; correlation coefficients (R-2) were only 0.926 and 0.947, for CBH I and II, respectively. The experimental isotherms were best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation); using these models the correlation coefficients were in most cases higher than 0.995. Apparent binding parameters derived from the two sites Langmuir model indicated stronger binding of CBH II compared to CBH I; the distribution coefficients were 20.7 and 3.7 L/g for the two enzymes, respectively. The binding capacity, on the other hand, was higher for CBH I, 1.0 mu mol (67 mg) per gram Avicel, compared to 0.57 mu mol/g (30 mg/g) for CBH II. The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules.},
  author       = {Medve, J and Ståhlberg, J and Tjerneld, Folke},
  issn         = {1559-0291},
  keyword      = {SYNERGISM,COMPONENTS,CELLULASES,ENZYMATIC-HYDROLYSIS,LIQUID-CHROMATOGRAPHIC SORBENTS,2 CELLOBIOHYDROLASES,DOMAIN,VIRIDE,EQUILIBRIA,PROTEINS},
  language     = {eng},
  number       = {1},
  pages        = {39--56},
  publisher    = {Humana Press},
  series       = {Applied Biochemistry and Biotechnology},
  title        = {Isotherms for adsorption of cellobiohydrolase I and II from Trichoderma reesei on microcrystalline cellulose},
  url          = {http://dx.doi.org/10.1007/BF02788806},
  volume       = {66},
  year         = {1997},
}