Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins
Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins fro...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-04-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/10/4/796 |
| _version_ | 1797538486453010432 |
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| author | David J. Andlinger Pauline Röscheisen Claudia Hengst Ulrich Kulozik |
| author_facet | David J. Andlinger Pauline Röscheisen Claudia Hengst Ulrich Kulozik |
| author_sort | David J. Andlinger |
| collection | DOAJ |
| description | Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. In this work, the influence of pH and temperature on the kinetics of PPI denaturation and aggregation was investigated as an option for targeted functionalization. At a slightly acidic pH, rates of denaturation and aggregation of the globular patatin in PPI were fast. These aggregates were shown to possess a low amount of disulfide bonds and a high amount of exposed hydrophobic amino acids (S<sub>0</sub>). Gradually increasing the pH slowed down the rate of denaturation and aggregation and alkaline pH levels led to an increased formation of disulfide bonds within these aggregates, whereas S<sub>0</sub> was reduced. Aggregation below denaturation temperature (T<sub>d</sub>) favored aggregation driven by disulfide bridge formation. Aggregation above T<sub>d</sub> led to fast unfolding, and initial aggregation was less determined by disulfide bridge formation. Inter-molecular disulfide formation occurred during extended heating times. Blocking different protein interactions revealed that the formation of disulfide bond linked aggregation is preceded by the formation of non-covalent bonds. Overall, the results help to control the kinetics, morphology, and interactions of potato protein aggregation for potential applications in food systems. |
| first_indexed | 2024-03-10T12:31:04Z |
| format | Article |
| id | doaj.art-95c5667b6f5e4eea84fff5aae1a5a321 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T12:31:04Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-95c5667b6f5e4eea84fff5aae1a5a3212023-11-21T14:38:33ZengMDPI AGFoods2304-81582021-04-0110479610.3390/foods10040796Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato ProteinsDavid J. Andlinger0Pauline Röscheisen1Claudia Hengst2Ulrich Kulozik3Food and Bioprocess Engineering, TUM School of Life Sciences, Technical University of Munich, Weihenstephaner Berg 1, 85354 Freising, GermanyFood and Bioprocess Engineering, TUM School of Life Sciences, Technical University of Munich, Weihenstephaner Berg 1, 85354 Freising, GermanyFood and Bioprocess Engineering, TUM School of Life Sciences, Technical University of Munich, Weihenstephaner Berg 1, 85354 Freising, GermanyFood and Bioprocess Engineering, TUM School of Life Sciences, Technical University of Munich, Weihenstephaner Berg 1, 85354 Freising, GermanyUnderstanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. In this work, the influence of pH and temperature on the kinetics of PPI denaturation and aggregation was investigated as an option for targeted functionalization. At a slightly acidic pH, rates of denaturation and aggregation of the globular patatin in PPI were fast. These aggregates were shown to possess a low amount of disulfide bonds and a high amount of exposed hydrophobic amino acids (S<sub>0</sub>). Gradually increasing the pH slowed down the rate of denaturation and aggregation and alkaline pH levels led to an increased formation of disulfide bonds within these aggregates, whereas S<sub>0</sub> was reduced. Aggregation below denaturation temperature (T<sub>d</sub>) favored aggregation driven by disulfide bridge formation. Aggregation above T<sub>d</sub> led to fast unfolding, and initial aggregation was less determined by disulfide bridge formation. Inter-molecular disulfide formation occurred during extended heating times. Blocking different protein interactions revealed that the formation of disulfide bond linked aggregation is preceded by the formation of non-covalent bonds. Overall, the results help to control the kinetics, morphology, and interactions of potato protein aggregation for potential applications in food systems.https://www.mdpi.com/2304-8158/10/4/796patatinthiolsulfhydryl grouphydrophobicnon-linear regressiondenaturation |
| spellingShingle | David J. Andlinger Pauline Röscheisen Claudia Hengst Ulrich Kulozik Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins Foods patatin thiol sulfhydryl group hydrophobic non-linear regression denaturation |
| title | Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins |
| title_full | Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins |
| title_fullStr | Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins |
| title_full_unstemmed | Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins |
| title_short | Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins |
| title_sort | influence of ph temperature and protease inhibitors on kinetics and mechanism of thermally induced aggregation of potato proteins |
| topic | patatin thiol sulfhydryl group hydrophobic non-linear regression denaturation |
| url | https://www.mdpi.com/2304-8158/10/4/796 |
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