Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 100, Issue 10, Pages 4435-4446Publisher
SPRINGER
DOI: 10.1007/s00253-015-7254-1
Keywords
Cutinase; Surface charge; Substrate binding; Glycosylation; Biochemical characterization; Polyester hydrolysis
Categories
Funding
- National Science Foundation's Chemical, Bioengineering, Environmental and Transport Systems (CBET) Division [1067415]
- NIH [R01 GM099827]
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1067415] Funding Source: National Science Foundation
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Cutinases are esterases of industrial importance for applications in recycling and surface modification of polyesters. The cutinase from Thielavia terrestris (TtC) is distinct in terms of its ability to retain its stability and activity in acidic pH. Stability and activity in acidic pHs are desirable for esterases as the pH of the reaction tends to go down with the generation of acid. The pH stability and activity are governed by the charged state of the residues involved in catalysis or in substrate binding. In this study, we performed the detailed structural and biochemical characterization of TtC coupled with surface charge analysis to understand its acidic tolerance. The stability of TtC in acidic pH was rationalized by evaluating the contribution of charge interactions to the Gibbs free energy of unfolding at varying pHs. The activity of TtC was found to be limited by substrate binding affinity, which is a function of the surface charge. Additionally, the presence of glycosylation affects the biochemical characteristics of TtC owing to steric interactions with residues involved in substrate binding.
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