Optimising biocatalyst design for obtaining high transesterification activity by α-chymotrypsin in non-aqueous media
2008
Improving Enzyme Activity in Organic Solvents
publication
Evidence: moderate
Author Information
Author(s): Kusum Solanki, Munishwar Nath Gupta
Primary Institution: Indian Institute of Technology Delhi
Hypothesis
The presence of trehalose enhances the transesterification activity of α-chymotrypsin in non-aqueous media.
Conclusion
The study found that trehalose significantly increases the transesterification rates of α-chymotrypsin in organic solvents.
Supporting Evidence
- EPRPs with trehalose showed transesterification rates of 45.2 nmoles mg-1min-1 compared to 16.6 nmoles mg-1min-1 without trehalose.
- The presence of trehalose resulted in smaller enzyme particle sizes, which may contribute to higher activity.
- PCMCs prepared with trehalose exhibited higher initial rates than EPRPs.
Takeaway
Adding trehalose helps an enzyme work better in dry environments, making it faster at its job.
Methodology
The study involved preparing enzyme preparations with and without trehalose and measuring their transesterification activity in different organic solvents.
Limitations
The study did not explore the long-term stability of the enzyme preparations in organic solvents.
Digital Object Identifier (DOI)
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