Bridging the Knowledge Gap for the Impact of Non-Thermal Processing on Proteins and Amino Acids

被引:45
作者
Esteghlal, Sara [1 ,2 ]
Gahruie, Hadi Hashemi [1 ,2 ]
Niakousari, Mehrdad [1 ]
Barba, Francisco J. [3 ]
Bekhit, Alaa El-Din [4 ]
Mallikarjunan, Kumar [5 ]
Roohinejad, Shahin [5 ,6 ]
机构
[1] Shiraz Univ, Sch Agr, Dept Food Sci & Technol, Shiraz, Iran
[2] Shiraz Univ, Sch Agr, Dept Food Sci & Technol, Biomol Engn Lab, Shiraz, Iran
[3] Univ Valencia, Fac Pharm, Food Sci Toxicol & Forens Med Dept, Nutr & Food Sci Area,Prevent Med & Publ Hlth, Avda Vicent Andres Estelles S-N, E-46100 Valencia, Spain
[4] Univ Otago, Dept Food Sci, Dunedin 9054, New Zealand
[5] Univ Minnesota, Dept Food Sci & Nutr, St Paul, MN 55108 USA
[6] Shiraz Univ Med Sci, Div Food & Nutr, Burn & Wound Healing Res Ctr, Shiraz, Iran
基金
欧盟地平线“2020”;
关键词
Irradiation; ultrasound; cold plasma; pulsed electric fields; high-pressure processing; proteins and amino acids; PULSED ELECTRIC-FIELDS; HIGH-HYDROSTATIC-PRESSURE; HIGH-INTENSITY ULTRASOUND; GAMMA-IRRADIATION; EMULSIFYING PROPERTIES; MYOFIBRILLAR PROTEIN; PHYSICOCHEMICAL PROPERTIES; STRUCTURAL-PROPERTIES; BETA-LACTOGLOBULIN; FOOD-SCIENCE;
D O I
10.3390/foods8070262
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.
引用
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页数:22
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