NDLI: Isotherms for adsorption of cellobiohydrolase I and II fromtrichoderma reesei on microcrystalline cellulose

Content Provider	Springer Nature Link
Author	Medve, József Ståhlberg, Jerry Tjerneld, Folke
Copyright Year	1997
Abstract	Adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I and II (CBH I and CBH II) fromTrichoderma reesei has been studied. Adsorption isotherms of the enzymes were measured at 4‡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 Μmol (67 mg) per gram Avicel, compared to 0.57 Μmol/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.
Starting Page	39
Ending Page	56
Page Count	18
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	66
Issue Number	1
e-ISSN	15590291
Language	English
Publisher	Humana Press
Publisher Date	1997-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Hydrolysis of steam-pretreated lignocellulose : Synergism and adsorption for cellobiohydrolase I and endogulcanase II of trichoderma reesei

Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow

Adsorption of Thermomonospora fusca E$_{5}$ and Trichoderma reesei cellobiohydrolase I cellulases on synthetic surfaces

A polyclonal antiserum to the noncatalytic part of cellobiohydrolase I fromTrichoderma reesei

Expression of Trichoderma reesei exo-cellobiohydrolase I in transgenic tobacco leaves and calli

Ionic strength effect on adsorption of cellobiohydrolases I and II on microcrystalline cellulose

A model explaining declining rate in hydrolysis of lignocellulose substrates with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) of Trichoderma reesei

Functional display of fungal cellulases from Trichoderma reesei on phage M13

Enhanced enzymatic cellulose degradation by cellobiohydrolases via product removal

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

Similar Documents

Hydrolysis of steam-pretreated lignocellulose : Synergism and adsorption for cellobiohydrolase I and endogulcanase II of trichoderma reesei

Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow

Adsorption of Thermomonospora fusca E$_{5}$ and Trichoderma reesei cellobiohydrolase I cellulases on synthetic surfaces

A polyclonal antiserum to the noncatalytic part of cellobiohydrolase I fromTrichoderma reesei

Expression of Trichoderma reesei exo-cellobiohydrolase I in transgenic tobacco leaves and calli

Ionic strength effect on adsorption of cellobiohydrolases I and II on microcrystalline cellulose

A model explaining declining rate in hydrolysis of lignocellulose substrates with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) of Trichoderma reesei

Functional display of fungal cellulases from Trichoderma reesei on phage M13

Enhanced enzymatic cellulose degradation by cellobiohydrolases via product removal

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