AI Summary
The research study successfully enhanced the thermostability of carboxypeptidase A (CPA) through the introduction of disulfide bonds, allowing for broader industrial applications in processes that require high temperatures, such as degrading ochratoxin A and reducing bitterness in food peptides. This advancement in enzyme engineering using rational design strategies has the potential to improve efficiency, reduce production costs, and expand the use of CPA in various industries.
A research team has successfully enhanced the thermostability of carboxypeptidase A (CPA), a crucial enzyme with significant potential in the food and pharmaceutical industries, through the innovative use of disulfide bonds. This development promises to expand the enzyme’s use in processes that require high-temperature conditions, such as degrading ochratoxin A (OTA) and reducing the bitterness of peptides in food.
Carboxypeptidase A (CPA) is widely used in the food and pharmaceutical industries for its ability to hydrolyze toxic ochratoxin A (OTA) into non-toxic compounds and remove bitterness from peptides in food processing. However, CPA’s natural mesophilic nature limits its function at higher temperatures, restricting its application in industrial settings where elevated heat is common.
Enzyme thermostability is essential for extending operational temperatures, improving efficiency, and reducing production costs. Previous efforts to enhance enzyme thermostability have shown that protein engineering, particularly the introduction of disulfide bonds, can significantly stabilize enzymes for industrial use.
The study published in Food Innovation and Advances on 25 June 2024, marks a significant leap forward in enzyme engineering.
The research utilized a rational design strategy to enhance the thermostability of Carboxypeptidase A (CPA) by introducing disulfide bonds. First, flexible regions of CPA were identified using B-factor analysis, which characterizes thermal motion in proteins, and RMSF values,