Catalytic peptide synthesis by trypsin modified with polystyrene in chloroform

Area of Science:

• Biochemistry
• Polymer Chemistry
• Enzyme Engineering

Background:

• Enzyme modification is crucial for expanding their application range.
• Hydrophobic polymers can alter enzyme solubility and stability.
• Polystyrene is a common synthetic hydrophobic polymer.

Purpose of the Study:

• To covalently attach polystyrene to trypsin.
• To assess the retained catalytic activity of modified trypsin in a hydrophobic solvent.
• To investigate the stereoselectivity of the modified enzyme's catalytic reaction.

Main Methods:

• Trypsin was functionalized with azo-bis(4-cyano-valeric acid) via its amine groups.
• Styrene polymerization was initiated by the azo initiator in the presence of modified trypsin.
• The modified trypsin's enzymatic activity was tested in chloroform by catalyzing peptide bond formation.

Main Results:

• Successful covalent attachment of polystyrene to trypsin was achieved.
• Modified trypsin demonstrated retained catalytic activity in chloroform.
• The enzyme-catalyzed peptide formation exhibited stereoselectivity.

Conclusions:

• Covalent attachment of polystyrene to trypsin preserves its enzymatic function in hydrophobic environments.
• This modification enables enzyme catalysis in non-aqueous solvents like chloroform.
• The modified trypsin maintains stereoselectivity, indicating potential for chiral synthesis applications.