Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour
Plant proteins have become increasingly desirable due to their sustainability and proposed health benefits. This study initially examined the effects of heat treatment on the solubility of pea protein (PP) in a 3 % (w/w) protein solution, applying heat from 65 °C to 95 °C for varying durations acros...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-01-01
|
| Series: | Current Research in Food Science |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2665927125002047 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849229210611089408 |
|---|---|
| author | Dan Li Ying Ma Alejandra Acevedo-Fani Weihong Lu Harjinder Singh Aiqian Ye |
| author_facet | Dan Li Ying Ma Alejandra Acevedo-Fani Weihong Lu Harjinder Singh Aiqian Ye |
| author_sort | Dan Li |
| collection | DOAJ |
| description | Plant proteins have become increasingly desirable due to their sustainability and proposed health benefits. This study initially examined the effects of heat treatment on the solubility of pea protein (PP) in a 3 % (w/w) protein solution, applying heat from 65 °C to 95 °C for varying durations across pH conditions ranging from 5.5 to 7.8. Subsequently, an advanced dynamic gastric digestion model—the Human Gastric Simulator—was employed to examine the in vitro gastric digestion behaviours of heat-treated and untreated PP. Results suggest that heat treatment reduces the protein aggregate size and enhances PP solubility, potentially due to a decrease in α-helix and β-turn structures or an increase in β-sheet content, as determined via Fourier transform infrared spectroscopy. Additionally, heat treatment elevated the surface hydrophobicity and free sulfhydryl group concentration of PP. During in vitro dynamic gastric digestion with pepsin, PP underwent notable structural and physical stability modifications. Unheated and heated PP exhibited small particles in the digesta and remained unaggregated throughout digestion. However, the heat-treated PP showed a smaller particle size during gastric digestion and a greater hydrolysis rate than the unheated protein. This study systematically evaluates the solubility and digestion behaviour of PP subjected to food processing conditions, highlighting its stability and structural changes that may influence the delivery of macronutrients from the stomach to the next phase of digestion. |
| format | Article |
| id | doaj-art-07e5e85228764df790bf5e44db36fd7f |
| institution | Kabale University |
| issn | 2665-9271 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Current Research in Food Science |
| spelling | doaj-art-07e5e85228764df790bf5e44db36fd7f2025-08-22T04:58:10ZengElsevierCurrent Research in Food Science2665-92712025-01-011110117310.1016/j.crfs.2025.101173Heat-induced modifications of pea protein: Implications for solubility and digestion behaviourDan Li0Ying Ma1Alejandra Acevedo-Fani2Weihong Lu3Harjinder Singh4Aiqian Ye5Riddet Institute, Massey University, Private Bag 11 222, Palmerston North, 4442, New Zealand; School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin, 150001, ChinaSchool of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin, 150001, ChinaRiddet Institute, Massey University, Private Bag 11 222, Palmerston North, 4442, New ZealandSchool of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin, 150001, ChinaRiddet Institute, Massey University, Private Bag 11 222, Palmerston North, 4442, New ZealandRiddet Institute, Massey University, Private Bag 11 222, Palmerston North, 4442, New Zealand; Corresponding author.Plant proteins have become increasingly desirable due to their sustainability and proposed health benefits. This study initially examined the effects of heat treatment on the solubility of pea protein (PP) in a 3 % (w/w) protein solution, applying heat from 65 °C to 95 °C for varying durations across pH conditions ranging from 5.5 to 7.8. Subsequently, an advanced dynamic gastric digestion model—the Human Gastric Simulator—was employed to examine the in vitro gastric digestion behaviours of heat-treated and untreated PP. Results suggest that heat treatment reduces the protein aggregate size and enhances PP solubility, potentially due to a decrease in α-helix and β-turn structures or an increase in β-sheet content, as determined via Fourier transform infrared spectroscopy. Additionally, heat treatment elevated the surface hydrophobicity and free sulfhydryl group concentration of PP. During in vitro dynamic gastric digestion with pepsin, PP underwent notable structural and physical stability modifications. Unheated and heated PP exhibited small particles in the digesta and remained unaggregated throughout digestion. However, the heat-treated PP showed a smaller particle size during gastric digestion and a greater hydrolysis rate than the unheated protein. This study systematically evaluates the solubility and digestion behaviour of PP subjected to food processing conditions, highlighting its stability and structural changes that may influence the delivery of macronutrients from the stomach to the next phase of digestion.http://www.sciencedirect.com/science/article/pii/S2665927125002047Pea protein isolateHeat treatmentProtein solubilityHydrolysisGastric emptyingProtein digestibility |
| spellingShingle | Dan Li Ying Ma Alejandra Acevedo-Fani Weihong Lu Harjinder Singh Aiqian Ye Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour Current Research in Food Science Pea protein isolate Heat treatment Protein solubility Hydrolysis Gastric emptying Protein digestibility |
| title | Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour |
| title_full | Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour |
| title_fullStr | Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour |
| title_full_unstemmed | Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour |
| title_short | Heat-induced modifications of pea protein: Implications for solubility and digestion behaviour |
| title_sort | heat induced modifications of pea protein implications for solubility and digestion behaviour |
| topic | Pea protein isolate Heat treatment Protein solubility Hydrolysis Gastric emptying Protein digestibility |
| url | http://www.sciencedirect.com/science/article/pii/S2665927125002047 |
| work_keys_str_mv | AT danli heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour AT yingma heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour AT alejandraacevedofani heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour AT weihonglu heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour AT harjindersingh heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour AT aiqianye heatinducedmodificationsofpeaproteinimplicationsforsolubilityanddigestionbehaviour |