Abstract
The conversion of barley starch to sugars is a complex enzymic process. Most previous work concerned the biotechnical aspect of in situ barley enzymes. However, the interactions among the macromolecular substrates and their effects on enzymic catalysis has been little examined. Here, we explore the mechanisms whereby interactions of protein and starch in barley flour affect the kinetics of enzymatic hydrolysis of starch in an in vitro system, using digestion rate data and structural analysis by confocal microscopy. The degradation kinetics of both uncooked barley flour and of purified starches are found to be two-step sequential processes. Barley proteins, especially the water-soluble component, are found to retard the digestion of starch degraded by α-amylase: the enzyme binds with water-insoluble protein and with starch granules, leading to reduced starch hydrolysis. These findings are of potential industrial value in both the brewing and food industries.
Original language | English |
---|---|
Pages (from-to) | 493-501 |
Number of pages | 9 |
Journal | Food Chemistry |
Volume | 241 |
DOIs | |
Publication status | Published - 15 Feb 2018 |
Externally published | Yes |
Keywords
- Barley (hordeum vulgare L.)
- Confocal microscopy
- Enzyme activity
- Enzyme binding
- In vitro hydrolysis
- Starch digestibility