Comparative Characterization of Oxidative Enzymes for Arabinoxylan and Protein Cross-Linking via Ferulic Acid and Tyrosine in Model Systems

Summary

Scientists tested different enzymes to see which ones work best at linking proteins and fiber molecules together in bread dough. They found that combining certain enzymes, especially peroxidase with glucose oxidase, works better than using them alone. By adjusting the amounts of ferulic acid and tyrosine (compounds in food), they could control whether the cross-links formed within the same molecule or between different molecules. This research helps food makers choose the right enzymes to improve bread texture without extra processing steps.

Background

Cross-linking enzymes are commonly used in food processing, particularly in gluten-free bread formulations, to improve dough properties. Oxidoreductases such as laccase, peroxidase, tyrosinase, and glucose oxidase can facilitate covalent cross-links between proteins and arabinoxylans through oxidation of phenolic compounds and amino acids.

Objective

This study comparatively investigated various oxidoreductases and their combinations for their ability to convert tyrosine in proteins and ferulic acid in arabinoxylans as cross-linking tools. The research aimed to establish a basis for rational enzyme selection for food structure improvements.

Results

Enzyme characteristics varied significantly across assays with substrate-dependent shifts in pH optima. Enzyme combinations altered kinetic parameters; combining peroxidase with glucose oxidase reduced Km for ferulic acid from 0.250 to 0.045 mM. The substrate ratio was crucial for targeting homo- or heterocross-linking, with the most effective simultaneous conversion achieved at a 1:5 (ferulic acid:tyrosine) ratio.

Conclusion

The study provides valuable insights into oxidoreductase cross-linking behavior in MS-compatible buffer systems. Findings support rational enzyme selection strategies for improving food structure through biocatalytic cross-linking of biopolymers.
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