Next Article in Journal
In Vitro Ecological Response of the Human Gut Microbiome to Bioactive Extracts from Edible Wild Mushrooms
Previous Article in Journal
Probing the Anticancer Action of Novel Ferrocene Analogues of MNK Inhibitors
Open AccessArticle

Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate

School of Food Engineering, Harbin University of Commerce, Harbin 150076, China
Food Processing Institute, Heilongjiang Academy of Agricultural Sciences, Harbin 150086, China
Academy of Quality Inspection and Research in Heilongjiang Province, Harbin 150050, China
College of Engineering, Northeast Agricultural University, Harbin 150030, China
Author to whom correspondence should be addressed.
Molecules 2018, 23(9), 2127;
Received: 5 July 2018 / Revised: 19 August 2018 / Accepted: 22 August 2018 / Published: 23 August 2018
To explore better methods of natural protein modification for black soybean, comparisons among the effects of different modified methods on structural changes of the modified products of black soybean protein isolate (BSPI) were carried out in this study. The modified products used in this study included enzymatic crossing-link black soybean protein isolate (ECBSPI), wet heating treatment glycosylation black soybean protein isolate (WHTGBSPI) and especially enzymatic glycosylation black soybean protein isolate catalyzed by transglutaminase (EGBSPI). The effects of the modification methods on structural changes were analyzed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), amino acid content and circular dichroism (CD) analysis. Moreover, the processing properties changes caused by structural changes of BSPI were detected by thermogravimetric analysis, particle size analysis, zeta-potential, surface hydrophobicity, solubility, emulsification, gelation, and rheological properties. The results show that the modified BSPI products were protein polymers, and among them, EGBSP and WHTGBSPI are covalently bonded glycation products. Products modified by Maillard reactions and transglutaminase (TG) display partly destroyed α-helix and β-sheet structures that form more open secondary BSPI structures. For ECBSPI, the proportion of irregular crimp structure reduces to form a high order secondary structure. All the modified products form fine aggregations in dispersion, except WHTGBSPI has most negative zeta-potential and least molecular stability due to the hydrophobic amino acids embedded in the protein molecules. The zeta-potentials of BSPI, ECBSPI, WHTGBSPI and EGBSPI are respectively −21.5, −23.8, −18.1 and −20.2 mV. The surface hydrophobicity of EGBSPI (5.07 ± 0.07) and WHTGBSPI (7.02 ± 0.05) decrease, while the surface hydrophobicity of ECBSPI (19.5 ± 0.06) increases. The solubility and rheological properties of EGBSPI, ECBSPI and WHTGBSPI after modification are all better than those of BSPI, especially EGBSPI. Emulsification of EGBSPI and WHTGBSPI increase (by 24.5% and 12.2%, respectively) while ECBSPI decrease (by 17.0), and there is similar emulsion stability trend. Moreover, the properties of ECBSPI increase except cohesiveness compared to BSPI. In conclusion, as a safe and efficient method for natural protein modification, enzymatic glycosylation catalyzed by TG has great potential in improving food processing characteristics. View Full-Text
Keywords: black soybean protein isolate; transglutaminase (TG); Maillard reaction; modification; structure black soybean protein isolate; transglutaminase (TG); Maillard reaction; modification; structure
Show Figures

Figure 1

MDPI and ACS Style

Zhang, Y.; Yin, Y.; Lu, S.; Yao, X.; Zheng, X.; Zhao, R.; Li, Z.; Shen, H.; Zhang, S. Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate. Molecules 2018, 23, 2127.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Search more from Scilit
Back to TopTop