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Published on: February 21, 2019
Identification and characterization of bacterial cutinase
Sheng Chen1, Xing Tong, Ronald W Woodard
1State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Ave., Wuxi, Jiangsu 214122, China.
The Journal of Biological Chemistry
|July 29, 2008
Summary
This study identifies and characterizes bacterial cutinases from Thermobifida fusca, revealing their enzymatic properties and thermal stability. These findings advance our understanding of bacterial cutinase genes and their potential applications.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Cutinases catalyze ester bond cleavage in cutin, with fungal enzymes extensively studied.
- Bacterial cutinase research is limited due to challenges in identifying their encoding genes.
Purpose of the Study:
- To identify and characterize bacterial cutinases from Thermobifida fusca.
- To compare the properties of bacterial cutinases with fungal counterparts.
Main Methods:
- Enzyme induction by cutin and purification based on p-nitrophenyl butyrate hydrolysis.
- Peptide mass fingerprinting to identify enzyme-encoding genes.
- Cloning, overexpression, and comparative enzymatic characterization.
Main Results:
- Identified two homologous proteins (Tfu_0883, Tfu_0882) as Thermobifida fusca cutinases.
- Confirmed cutinase activity through ester bond hydrolysis of cutin.
- Demonstrated higher thermal stability in T. fusca cutinases compared to fungal cutinases.
- Revealed an alpha/beta-hydrolase fold and a serine hydrolase catalytic mechanism.
Conclusions:
- This is the first report of bacterial cutinase-encoding genes.
- T. fusca cutinases exhibit distinct properties, including enhanced thermal stability.
- Findings provide insights into bacterial cutinase structure, function, and potential applications.
