Preparation of enzymatically cross-linked α-lactalbumin nanoparticles and their application for encapsulating lycopene

Siqi Guo; Qing Guo; Yifan Zhang; Xiaoke Peng; Cuicui Ma; David Julian McClements; Xuebo Liu; Fuguo Liu

doi:10.1016/j.foodchem.2023.136394

Preparation of enzymatically cross-linked α-lactalbumin nanoparticles and their application for encapsulating lycopene

Food Chem. 2023 Dec 15:429:136394. doi: 10.1016/j.foodchem.2023.136394. Epub 2023 May 17.

Authors

Siqi Guo¹, Qing Guo², Yifan Zhang³, Xiaoke Peng³, Cuicui Ma³, David Julian McClements⁴, Xuebo Liu³, Fuguo Liu⁵

Affiliations

¹ College of Food Science and Engineering, Northwest A&F University, Yangling 712100, Shaanxi, China; College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China.
² State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Tianjin 300457, China.
³ College of Food Science and Engineering, Northwest A&F University, Yangling 712100, Shaanxi, China.
⁴ Department of Food Science, University of Massachusetts, Amherst, MA 01003, United States.
⁵ College of Food Science and Engineering, Northwest A&F University, Yangling 712100, Shaanxi, China. Electronic address: fuguo@nwafu.edu.cn.

PMID: 37478605
DOI: 10.1016/j.foodchem.2023.136394

Abstract

High internal phase Pickering emulsions (HIPPEs) stabilized by protein nanoparticles have been widely reported, but the use of enzymatic methods for preparing these nanoparticles remains underexplored. Our hypothesis is that enzymatically crosslinked α-lactalbumin (ALA) nanoparticles (ALATGs) prepared using transglutaminase will demonstrate improved properties as stabilizers for HIPPEs. In this study, we investigated the physicochemical properties and microstructures of ALATGs, finding that enzymatic crosslinking could be enhanced by removing Ca²⁺ ions from ALA and preheating the proteins (85 °C, 15 min). The electrical charge, secondary structure, and surface hydrophobicity of ALATGs were found to depend on crosslinking conditions. HIPPEs formed with an ALA concentration of 10 mg/mL and an enzyme activity of 120 U/g exhibited the highest apparent viscosity and mechanical strength, as well as significantly improved loading capacity and photostability for the encapsulated lycopene. Overall, our results support the hypothesis that ALATG-nanoparticles show superior performance as emulsifiers compared to ALA-nanoparticles.

Keywords: High internal phase Pickering emulsion; Nanoparticles; Transglutaminase; α-Lactalbumin.

MeSH terms

Emulsions / chemistry
Hydrophobic and Hydrophilic Interactions
Lactalbumin* / chemistry
Lycopene
Nanoparticles* / chemistry
Particle Size
Transcription Factors

Substances

Lactalbumin
Lycopene
Emulsions
Transcription Factors