Hesperidinase encapsulation towards hesperitin production targeting improved bioavailability

Area of Science:

• Biocatalysis and Enzyme Engineering
• Flavonoid Chemistry
• Biotechnology

Background:

• Hesperidin and hesperitin possess beneficial health effects, including anti-inflammatory and antioxidant properties.
• Hesperidin exhibits low bioavailability due to its glycosidic structure, limiting its therapeutic potential.
• Hesperitin, the aglycone of hesperidin, offers improved bioavailability and similar health benefits.

Purpose of the Study:

• To develop an enzymatic process for producing hesperitin from hesperidin using hesperidinase.
• To investigate the immobilization of hesperidinase on various hydrogels to enhance its stability and efficiency.
• To optimize the bioconversion process for hesperitin production, particularly with insoluble hesperidin substrate.

Main Methods:

• Enzymatic bioconversion of hesperidin to hesperitin using hesperidinase.
• Immobilization of hesperidinase via adsorption and encapsulation in calcium alginate, k-carrageenan, and chitosan beads.
• Cross-linking of chitosan beads with glutaraldehyde and sodium sulfate.
• Evaluation of enzyme stability and activity under different immobilization conditions.

Main Results:

• Enzymatic degradation of insoluble hesperidin was observed, with increased reaction rates.
• Immobilized hesperidinase showed a residual activity of 193% compared to the soluble form.
• Hesperidinase encapsulated in calcium alginate beads achieved a half-life of 770 minutes, demonstrating enhanced stability.

Conclusions:

• Enzyme immobilization on hydrogels, particularly calcium alginate, significantly enhances hesperidinase stability and efficiency for hesperitin production.
• This approach offers a promising strategy for the large-scale enzymatic production of hesperitin from hesperidin.
• The improved hesperitin production method has significant implications for pharmaceutical and nutraceutical industries due to hesperitin's higher bioavailability.