Optimization of Soybean Protein Extraction Using By-Products from NaCl Electrolysis as an Application of the Industrial Symbiosis Concept

被引:7
|
作者
Ovando, Emilio [1 ]
Rodriguez-Sifuentes, Lucio [2 ]
Maria Martinez, Luz [1 ]
Chuck-Hernandez, Cristina [3 ]
机构
[1] Tecnol Monterrey, Sch Engn & Sci, Monterrey 64849, Mexico
[2] Univ Autonoma Coahuila, Fac Ciencias Biol, Torreon 27276, Mexico
[3] Tecnol Monterrey, Inst Obes Res, Monterrey 64849, Mexico
来源
APPLIED SCIENCES-BASEL | 2022年 / 12卷 / 06期
关键词
alkaline protein extraction; Box-Behnken design; electrolysis; hypochlorous acid; protein functional properties; soybean flour; soy protein isolate; MOLECULAR-STRUCTURE CHARACTERISTICS; SOY PROTEIN; FUNCTIONAL-PROPERTIES; EMULSIFYING PROPERTIES; FLOUR; FTIR; EXTRACTABILITY; DIGESTIBILITY; FORMULATION; DESIGN;
D O I
10.3390/app12063113
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Defatted soybean flour is generated during the oil extraction process of soybean, and it has a protein content of similar to 50%. On the other hand, an alkaline solution of NaOH is produced during the electrolysis process of NaCl in a novel method used to make a potent disinfectant/antiseptic (HOCl). In the present work, we suggest using these two products to produce soy protein isolate (SPI), aiming to create an industrial symbiosis. A Box-Behnken experimental design was executed, and a surface response analysis was performed to optimize temperature, alkaline solution, and time used for SPI extraction. The SPI produced at optimal conditions was then characterized. The experimental results fit well with a second-order polynomial equation that could predict 93.15% of the variability under a combination of 70 degrees C, alkaline solution 3 (pH 12.68), and 44.7 min of the process. The model predicts a 49.79% extraction yield, and when tested, we obtained 48.30% within the confidence interval (46.66-52.93%). The obtained SPI was comparable in content and structure with a commercial SPI by molecular weight and molecular spectroscopy characterization. Finally, the urease activity (UA) test was negative, indicating no activity for trypsin inhibitor. Based on the functional properties, the SPI is suitable for food applications.
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页数:16
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