Effects of xylooligosaccharide on angiotensin I-converting enzyme inhibitory activity of fish actomyosin and quality of snakehead balls with or without high hydrostatic pressure treatment

LWT(2021)

Cited 3|Views7
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Abstract
The interaction of fish actomyosin (AM) with high hydrostatic pressure (HHP) treatment (AM-HHP) and xylooligosaccharide (XOS) was analyzed. The binding force of AM/AM-HHP mainly binds with XOS was through hydrogen bonding and van der Waals forces. The interaction between AM-HHP and XOS was stronger than that between AM and XOS. The maximum binding affinity of AM-HHP and XOS was 400 MPa. The AM (400 MPa)-XOS complex had significantly enhanced angiotensin I-converting enzyme (ACE) inhibitory activity compared with the non-pressurized AM. Meanwhile, the negative influence of XOS on the ACE inhibitory activity of AM was significantly lesser than that of sucrose. ACE inhibitory activity was related to the surface hydrophobicity (H0) of the AM/AM-HHP-XOS complexes and the binding constant change of the AM-HHP-XOS interaction. In practical applications, 3% XOS addition in the snakehead balls with treatment at 400 MPa for 15 min increased the springiness of the fish ball by 1.32 times without changing its hardness. The above results indicate that XOS is an excellent food additive that could be used as a sucrose substitute in the HHP preparation of high-protein meat products.
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Key words
Actomyosin,Xylooligosaccharide,Interaction,ACE inhibitory Activity,Texture profile analysis
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