Effects of pine needle ice structuring protein on the functional properties of myofibrillar proteins from pork patty subjected to freezing-thawing cycles.

This study investigated the effects of pine needle ice structuring protein (PNISP, 0-0.8%, w/w) on physicochemical and functional properties of Myofibrillar proteins (MP) from pork patties under repeated freeze-thaw (F-T) cycles. Repeated F-T cycles significantly impaired MP functionality, including reduced solubility and surface charge, increased aggregation, weakened viscoelasticity, and deteriorated gel and emulsion stability. PNISP supplementation effectively alleviated these impairments, with 0.6% PNISP showing the optimal effect. PNISP-treated samples exhibited higher solubility, lower turbidity, finer particle distribution, and greater absolute ζ-potential than the control. PNISP also preserved higher storage modulus (G') and loss modulus (G″), stabilized the MP viscoelastic network, and improved gel strength, water-holding capacity, and emulsion stability with less water exudation. These effects were attributed to suppressed aggregation, enhanced colloidal stability, and stabilized intermolecular interactions. PNISP showed potential as a natural plant-derived cryoprotective agent for frozen meat products.