Effect of high-pressure homogenization optimized by response surface methodology on the techno-functional properties of protein concentrate isolated from date seed

被引:2
作者
Kelany, Mohamed A. [1 ,7 ,8 ]
Rashwan, Ahmed K. [2 ,3 ]
Kabil, Doaa I. [4 ]
Abdelshafy, Asem M. [5 ]
Osman, Ahmed I. [6 ]
El-Seedi, Hesham R. [9 ]
Yemis, Oktay [7 ,8 ]
机构
[1] Sohag Univ, Fac Agr, Dept Food Sci & Nutr, Sohag 82524, Egypt
[2] South Valley Univ, Fac Agr, Dept Food & Dairy Sci, Qena 83523, Egypt
[3] Zhejiang Univ, Coll Biosyst Engn & Food Sci, Dept Food Sci & Nutr, Hangzhou 310058, Peoples R China
[4] Tanta Univ, Fac Specif Educ, Home Econ Dept, Tanta 31527, Egypt
[5] Al Azhar Univ, Fac Agr, Dept Food Sci & Technol, Assiut Branch, Assiut 71524, Egypt
[6] Queens Univ Belfast, Sch Chem & Chem Engn, Belfast BT9 5AG, North Ireland
[7] Sakarya Univ, Fac Engn, Dept Food Engn, TR-54187 Sakarya, Turkiye
[8] Sakarya Univ, Res Dev & Applicat Ctr SARGEM, TR-54187 Sakarya, Turkiye
[9] Islamic Univ Madinah, Fac Sci, Chem Dept, Madinah 42351, Saudi Arabia
关键词
Date seed; Protein concentrate; High-pressure homogenization; Response surface methodology; Techno-functional properties; EMULSIFYING PROPERTIES; FOOD;
D O I
10.1016/j.indcrop.2024.119481
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
The study investigates the impact of high-pressure homogenization (HPH) optimized using response surface methodology (RSM) on the techno-functional properties of protein concentrate isolated from date seeds. The protein concentrate was subjected to HPH at various pressures (50, 100, and 150 MPa) and protein concentrations (1 %, 2 %, and 3 %) to optimize solubility, emulsifying activity, and antioxidant properties. RSM indicated optimal conditions at 150 MPa and 1 % protein concentration, resulting in significant enhancements in solubility (14.10 % to 43.69 %) and antioxidant activity (60.5 TE/g to 71.67 TE/g). The emulsifying activity index (EAI) increased from 11.92 m2/g 2 /g to 22.29 m2/g, 2 /g, though the emulsion stability index (ESI) slightly decreased from 17.63 min to 16.15 min. Besides, HPH improved oil-binding capacity (1.73 g/g to 3.02 g/g) while reducing water-binding capacity (2.76 g/g to 1.38 g/g). Structural analysis revealed that HPH caused partial protein unfolding and aggregation, indicated by changes in FTIR spectra, reduced fluorescence intensity, and increased surface sulfhydryl content (1.58 mu mol/g to 2.65 mu mol/g). These findings highlight HPH as an effective method to enhance the functional properties of date seed protein concentrate for potential applications in the food industry. In addition, the current study can lay a foundation for future HPH applications in other protein- rich by-products such as soybean cake, rapeseed cake, wheat bran, and others.
引用
收藏
页数:13
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