Comprehensive application possibility: Construction hydrophilic, amphiphilic and hydrophobic system of modified zein by enzymatic or cysteine modification. (February 2023)
- Record Type:
- Journal Article
- Title:
- Comprehensive application possibility: Construction hydrophilic, amphiphilic and hydrophobic system of modified zein by enzymatic or cysteine modification. (February 2023)
- Main Title:
- Comprehensive application possibility: Construction hydrophilic, amphiphilic and hydrophobic system of modified zein by enzymatic or cysteine modification
- Authors:
- Zhang, An-Qi
Li, Xiao-Yan
Liu, Bo-Hao
Yin, Yu-Qi
Zhang, Han-Lin
Zhang, Ying-Hua - Abstract:
- Abstract: Zein, a hydrophobic protein due to high percentage of apolar amino acids, which limits its modification and wide application in the food industry. The interaction between the molecule and water will be changed by introducing different hydrophilic groups into zein, which is the basis aimed at food application. Therefore, zein was modified based on construction of zein-potassium oleate system to obtain hydrophilic, amphiphilic and hydrophobic systems, thus the structure and properties of modified zein were explored in the present study. The results of the three-phase contact angle showed that the constructed zein-potassium oleate system is a hydrophobic system. After enzymatic modification, a hydrophilic system can be obtained. Amphiphilic system can be obtained by cysteine modification. Sodium dodecyl sulfate polyacrylamide gel electrophoresis, gel size exclusion chromatography, hydrophilic-lipophilic balance value, free amino group and sulfhydryl group results can also prove the hydrophilic and hydrophobic system obtained by different modification methods. Ultraviolet, Infrared and fluorescence spectra of zein after enzymatic hydrolysis and cysteine modification indicated that the hydrophilicity and hydrophobicity of the zein microenvironment also changed. This study may provide a feasible approach to broaden the application of zein in food industry. Graphical abstract: Image 1 Highlights: Two modification methods were used to realize the construction of differentAbstract: Zein, a hydrophobic protein due to high percentage of apolar amino acids, which limits its modification and wide application in the food industry. The interaction between the molecule and water will be changed by introducing different hydrophilic groups into zein, which is the basis aimed at food application. Therefore, zein was modified based on construction of zein-potassium oleate system to obtain hydrophilic, amphiphilic and hydrophobic systems, thus the structure and properties of modified zein were explored in the present study. The results of the three-phase contact angle showed that the constructed zein-potassium oleate system is a hydrophobic system. After enzymatic modification, a hydrophilic system can be obtained. Amphiphilic system can be obtained by cysteine modification. Sodium dodecyl sulfate polyacrylamide gel electrophoresis, gel size exclusion chromatography, hydrophilic-lipophilic balance value, free amino group and sulfhydryl group results can also prove the hydrophilic and hydrophobic system obtained by different modification methods. Ultraviolet, Infrared and fluorescence spectra of zein after enzymatic hydrolysis and cysteine modification indicated that the hydrophilicity and hydrophobicity of the zein microenvironment also changed. This study may provide a feasible approach to broaden the application of zein in food industry. Graphical abstract: Image 1 Highlights: Two modification methods were used to realize the construction of different systems of zein. The formation of different systems is directly or indirectly demonstrated in a number of ways. This paper provides a feasible approach to broaden the application of zein in food industry. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 135(2023)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 135(2023)
- Issue Display:
- Volume 135, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 135
- Issue:
- 2023
- Issue Sort Value:
- 2023-0135-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-02
- Subjects:
- Zein -- Hydrophilic systems -- Amphiphilic systems -- Hydrophobic systems -- Properties
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2022.108159 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 24211.xml