Publications by authors named "Guang-Qing Mu"

Article Synopsis
  • This study investigates how phospholipids interact with milk proteins in infant formula, focusing on phosphatidylcholine (PC) and whey protein isolate (WPI).
  • Findings suggest that as temperature increases, the binding strength between PC and WPI decreases, indicating a static quenching mechanism primarily driven by van der Waals forces and hydrogen bonds.
  • The research highlights that increasing PC concentration improves the emulsification properties of WPI, providing insights into practical applications in food technology.
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Lipids play a pivotal role in the nutrition of preterm infants, acting as a primary energy source. Due to their underdeveloped gastrointestinal systems, lipid malabsorption is common, leading to insufficient energy intake and slowed growth. Therefore, it is critical to explore the reasons behind the low lipid absorption rate in formulas for preterm infants.

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Whey protein concentrate (WPC) has been widely studied as a biodegradable bio-based packaging material in the food industry. In this study, different whey protein films were obtained through physical, chemical, enzymatic, and composite modifications. The molecular structure, micro-morphology, mechanical properties, barrier properties, and other characteristics of the films were evaluated.

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Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein.

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