Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 68, Issue 41, Pages 11535-11544Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.0c02059
Keywords
myofibrillar protein; gallic acid; cross-linking; soluble aggregate; thermal stability; protein beverage
Funding
- National Natural Science Foundation of China [31901611]
- Natural Science Foundation of Jiangsu Province, China [BK20190589]
- Fundamental Research Funds for the Central Universities, China [JUSRP11970]
- Youth Talent Support Project of Jiangsu Association for Science and Technology
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Low colloidal stability of myofibrillar protein (MP) during heating is a technofunctional constraint encountered in its beverage application. Gallic acid (GA), a natural polyphenol, was applied to fabricate MP soluble aggregates for an enhanced thermal stability. Upon pH shifting, GA was grafted into MP with the cysteine and tryptophan residues being the binding sites. As a result, the antioxidant activity of MP was enhanced. Additionally, GA modification decreased the a-helix structure of MP and converted MP into cross-linked aggregates. At low dosages (10 and 25 mu mol/g GA), disulfide-dominant covalent bonds were formed to generate myosin and actin aggregates, while MP aggregates were mostly bridged through GA-thiols or GA-tryptophan adducts when the dosages exceeded 50 mu mol/g. Such aggregates prevented MP from thermal gelation, leading to a stable and tunable colloidal state. This work can foster technological advances in the tailor manufacture of muscle protein-based beverages for special dietary uses.
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