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

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 inc...

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Autores principales: Zhang, Yinglei, Yin, Yanyang, Lu, Shuwen, Yao, Xinmiao, Zheng, Xianzhe, Zhao, Rui, Li, Zhebin, Shen, Huifang, Zhang, Shouwen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6225427/
https://www.ncbi.nlm.nih.gov/pubmed/30142966
http://dx.doi.org/10.3390/molecules23092127
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author Zhang, Yinglei
Yin, Yanyang
Lu, Shuwen
Yao, Xinmiao
Zheng, Xianzhe
Zhao, Rui
Li, Zhebin
Shen, Huifang
Zhang, Shouwen
author_facet Zhang, Yinglei
Yin, Yanyang
Lu, Shuwen
Yao, Xinmiao
Zheng, Xianzhe
Zhao, Rui
Li, Zhebin
Shen, Huifang
Zhang, Shouwen
author_sort Zhang, Yinglei
collection PubMed
description 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.
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spelling pubmed-62254272018-11-13 Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate Zhang, Yinglei Yin, Yanyang Lu, Shuwen Yao, Xinmiao Zheng, Xianzhe Zhao, Rui Li, Zhebin Shen, Huifang Zhang, Shouwen Molecules Article 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. MDPI 2018-08-23 /pmc/articles/PMC6225427/ /pubmed/30142966 http://dx.doi.org/10.3390/molecules23092127 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Yinglei
Yin, Yanyang
Lu, Shuwen
Yao, Xinmiao
Zheng, Xianzhe
Zhao, Rui
Li, Zhebin
Shen, Huifang
Zhang, Shouwen
Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title_full Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title_fullStr Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title_full_unstemmed Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title_short Effects of Modified Processing Methods on Structural Changes of Black Soybean Protein Isolate
title_sort effects of modified processing methods on structural changes of black soybean protein isolate
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6225427/
https://www.ncbi.nlm.nih.gov/pubmed/30142966
http://dx.doi.org/10.3390/molecules23092127
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