4.7 Article

Functional and bioactive properties of Larimichthys polyactis protein hydrolysates as influenced by plasma functionalized water-ultrasound hybrid treatments and enzyme types

Journal

ULTRASONICS SONOCHEMISTRY
Volume 86, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.ultsonch.2022.106023

Keywords

Alcalase; Papain; Chymotrypsin; Hydrolysis; Cavitation; Reactive oxygen species; Alcalase; Papain; Chymotrypsin; Hydrolysis; Cavitation; Reactive oxygen species

Funding

  1. National Natural Science Foundation of China [31972205]
  2. International S&T Cooperation Projects of Guangdong Province [2020A0505100007]
  3. Guangdong Basic and Applied Basic Research Foundation [2021A1515010644]
  4. Contemporary International Collaborative Research Centre of Guangdong Province on Food Innovative Processing and Intelligent Control [2019A050519001]
  5. Guangzhou Key Laboratory for Intelligent Sensing and Quality Control of Agricultural Products [202102100009]
  6. Common Technical Innovation Team of Guangdong Province on Preservation and Logistics of Agricultural Products [2021KJ145]
  7. China Scholarship Council [2018GXZ013452]

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The effects of plasma functionalized water (PFW) and its combination with ultrasound (UPFW) on the functional and bioactive properties of small yellow croaker protein hydrolysates (SYPHs) produced from three enzymes were investigated. The results showed that the treatments unfolded and denatured the protein molecules, resulting in improved enzymatic and antioxidant properties of the hydrolysates.
The effects of plasma functionalized water (PFW) and its combination with ultrasound (UPFW) on the functional and bioactive properties of small yellow croaker protein hydrolysates (SYPHs) produced from three enzymes were investigated. Fluorescence and UV-Vis spectroscopy indicated that SYPHs tended to unfold with increasing intensity and shift in wavelengths to more flexible conformations under PFW and UPFW treatments. Particle size distribution and microstructure analysis revealed that treatments could disrupt aggregation of protein molecules to increase the roughness, specific surface area, and decrease the particle size of peptides during hydrolysis. The partially denatured structure of SYPHs induced by treatments increased the susceptibility of the fish proteins to exogenous enzymes, thereby accelerating the hydrolytic process to yield peptides with improved solubility, decreased emulsifying and foaming properties, and improved enzyme-specific antioxidant properties. The results revealed that the functionality of SYPHs was influenced by the treatment method and the enzyme type employed.

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