Pectinase, a key enzyme widely used in food processing (e.g., juice clarification), still requires improvements in industrial stability and catalytic efficiency. Pectin oligosaccharides (POS), a specific degradation product of pectin, have attracted significant attention due to their exceptional prebiotic activity. However, conventional enzyme preparations often struggle to produce POS with the desired polymerization degree in a targeted and efficient manner.
To overcome this bottleneck, researchers employed protein engineering techniques to modify a fungal-derived endo-polygalacturonase. The study demonstrated that introducing cation-π interactions or cysteine site-directed mutations could significantly enhance the enzyme's thermal stability and catalytic efficiency. One successful modification increased the enzyme's melting temperature by 10 °C and boosted its activity by 36.5%.
Importantly, the mutant efficiently generated pectic oligosaccharides, which significantly promoted the growth of beneficial probiotics, demonstrating their prebiotic potential. These findings highlight the value of thermostable pectinases for industrial applications and advance the development of efficient enzymatic tools for prebiotic manufacturing and lay a solid scientific foundation for the large-scale production of high value-added functional food ingredients using biomass resources such as agricultural by-products.
The work entitled “Engineering of thermostable endo-polygalacturonase to generate prebiotic-active pectic oligosaccharides” was published on Systems Microbiology and Biomanufacturing (published on November 25, 2025).
DOI:10.1007/s43393-025-00404-w