NDLI: Structural Stability and Unfolding Properties of Cutinases from Thermobifida fusca

Content Provider	Springer Nature Link
Author	Hegde, Krishnamoorthy Dasu, Veeranki Venkata
Copyright Year	2014
Abstract	A comparative analysis of the structural and functional aspects along with equilibrium unfolding of two homologous cutinases, Cut1 and Cut2, from Thermobifida fusca was carried out. The CD and fluorescence profile at different pH in the range of 6 to 9 showed no structural variations for both cutinases, indicating their stability to a wide range of pH. Tryptophan quenching studies suggested that all the four Trp residues in the protein are in inaccessible hydrophobic pockets. Further, near-UV CD analysis of tertiary structure revealed a dissimilar distribution of aromatic amino acid on the surface of these two enzymes. Denaturation profiles obtained in aqueous solutions of the guanidine hydrochloride revealed different tolerance levels for unfolding of the two cutinases, with Cut2 showing higher resistivity to unfolding in comparison to Cut1. Both cutinases retained all the structural parameters even in the presence of 8 M urea, indicating the protein to be highly resistant to urea-induced unfolding. Structural study by homology modeling revealed a high resemblance of secondary structure between the two cutinases; however, their tertiary structure, hydrophobicity, and surface electrostatic properties were very different, which contributed to the difference in the structural stability of these two cutinases.
Starting Page	803
Ending Page	819
Page Count	17
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	174
Issue Number	2
e-ISSN	15590291
Language	English
Publisher	Springer US
Publisher Date	2014-08-07
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Circular dichroism Guanidine hydrochloride Homology modeling Protein denaturation Tryptophan fluorescence Cutinase Thermobifida fusca 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

Production Optimization and Characterization of Recombinant Cutinases from Thermobifida fusca sp. NRRL B-8184

Study on Improvement of Extracellular Production of Recombinant Thermobifida fusca Cutinase by Escherichia coli

Evidence for a Molten Globule State in Cicer α-Galactosidase Induced by pH, Temperature, and Guanidine Hydrochloride

Effects of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins on cotton bioscouring

Unfolding and Inactivation of Abalone (Haliotis diversicolor) Alkaline Phosphatase During Denaturation by Guanidine Hydrochloride

Calcium-induced stabilization of -amylase against guanidine hydrochloride denaturation

Carbohydrate binding and unfolding of Spatholobus parviflorus lectin: fluorescence and circular dichroism spectroscopic study.

Enhanced cutinase production of Thermobifida fusca by a two-stage batch and fed-batch cultivation strategy

Effects of guanidine hydrochloride on the conformation and enzyme activity of streptomycin adenylyltransferase monitored by circular dichroism and fluorescence spectroscopy

Structural Stability and Unfolding Properties of Cutinases from Thermobifida fusca

Similar Documents

Production Optimization and Characterization of Recombinant Cutinases from Thermobifida fusca sp. NRRL B-8184

Study on Improvement of Extracellular Production of Recombinant Thermobifida fusca Cutinase by Escherichia coli

Evidence for a Molten Globule State in Cicer α-Galactosidase Induced by pH, Temperature, and Guanidine Hydrochloride

Effects of Thermobifida fusca cutinase-carbohydrate-binding module fusion proteins on cotton bioscouring

Unfolding and Inactivation of Abalone (Haliotis diversicolor) Alkaline Phosphatase During Denaturation by Guanidine Hydrochloride

Calcium-induced stabilization of -amylase against guanidine hydrochloride denaturation

Carbohydrate binding and unfolding of Spatholobus parviflorus lectin: fluorescence and circular dichroism spectroscopic study.

Enhanced cutinase production of Thermobifida fusca by a two-stage batch and fed-batch cultivation strategy

Effects of guanidine hydrochloride on the conformation and enzyme activity of streptomycin adenylyltransferase monitored by circular dichroism and fluorescence spectroscopy

Structural Stability and Unfolding Properties of Cutinases from Thermobifida fusca