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Published on: May 25, 2018
Poly(aspartate) hydrolases: biochemical properties and applications.
Tomohiro Hiraishi1, Mizuo Maeda
1Bioengineering Laboratory, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. thiraish@riken.jp
Applied Microbiology and Biotechnology
|June 30, 2011
Summary
Thermally synthesized poly(aspartate) (tPAA) is a biodegradable polymer. Novel enzymes isolated from bacteria can break down tPAA and synthesize new β-peptides, offering green chemistry applications.
Area of Science:
- Green Polymer Chemistry
- Biotechnology
- Biochemistry
Background:
- Thermally synthesized poly(aspartate) (tPAA) offers a biodegradable alternative to conventional polycarboxylates.
- Understanding the structure-biodegradability relationship of tPAA is crucial for its application.
- Enzymatic synthesis presents a sustainable approach in polymer chemistry.
Purpose of the Study:
- To investigate the biodegradation of tPAA by identifying and characterizing specific enzymes.
- To explore the potential of these enzymes in synthesizing novel β-peptides for advanced materials.
Main Methods:
- Isolation and purification of two tPAA-degrading bacteria: Sphingomonas sp. KT-1 and Pedobacter sp. KP-2.
- Biological and genetic characterization of isolated PAA-hydrolyzing enzymes.
- Enzyme-catalyzed synthesis of poly(α-ethyl β-aspartate) using purified enzymes.
Main Results:
- Two novel PAA hydrolases were identified, capable of specifically cleaving the amide bond in tPAA.
- These enzymes play a key role in the biodegradation of tPAA by the isolated bacterial strains.
- The enzyme from Pedobacter sp. KP-2 was successfully used for the enzyme-catalyzed synthesis of poly(α-ethyl β-aspartate).
Conclusions:
- Novel enzymes capable of degrading tPAA and synthesizing β-peptides have been discovered.
- These enzymes demonstrate significant potential for applications in green polymer chemistry and the development of functional biomaterials.
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