Enhancement of the aspartame precursor synthetic activity of an organic solvent-stable protease

Protein Engineering, Design & Selection : PEDS
H OginoNoriyuki Doukyu

Abstract

The PST-01 protease is highly stable and catalyzes the synthesis of the aspartame precursor with high reaction yields in the presence of organic solvents. However, the synthesis rate using the PST-01 protease was slower than that observed when thermolysin was used. Structural comparison of both enzymes showed particular amino acid differences near the active center. These few residue differences in the PST-01 protease were mutated to match those amino acid types found in thermolysin. The mutated PST-01 proteases at the 114th residue from tyrosine to phenylalanine showed enhancement of synthetic activity. This activity was found to be similar to thermolysin. In addition, mutating the residue in the PST-01 protease with arginine and serine showed more improvement of the activity. The mutant PST-01 protease should be more useful than thermolysin for the synthesis of the aspartame precursor, because this enzyme has higher stability and activity in the presence of organic solvents. The results show the potential of organic solvent-stable enzymes as industrial catalysts.

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Citations

Apr 9, 2013·Applied Biochemistry and Biotechnology·Hamid Reza Karbalaei-HeidariGhodratollah Absalan
May 11, 2011·Chemical Reviews·Gernot A StrohmeierMandana Gruber-Khadjawi
Apr 4, 2012·Annual Review of Chemical and Biomolecular Engineering·Michael J LiszkaDouglas S Clark
Jun 20, 2014·ACS Medicinal Chemistry Letters·Gabriel BirraneManuel A Navia
Jan 1, 2013·Biomolecules·János András MótyánJózsef Tőzsér
Dec 6, 2017·Biotechnology & Genetic Engineering Reviews·Goutam Banerjee, Arun Kumar Ray
Jun 25, 2017·Journal of Industrial Microbiology & Biotechnology·Aneta M BiałkowskaTomasz Florczak

Related Concepts

NutraSweet
Enzyme Stability
Organic Chemicals
Peptide Hydrolases
Protein Conformation
Solvents
Substrate Specificity
Thermolysin
Protein Engineering
Mutagenesis, Site-Directed

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