Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties
Mung bean is a rich protein source, but its native form has limited solubility and functionality for food applications. As a promising agro-based crop, mung bean offers a sustainable alternative to traditional protein sources, especially in regions with limited access to resources. This study optimi...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-07-01
|
| Series: | Foods |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2304-8158/14/14/2459 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849409514159210496 |
|---|---|
| author | Kanokwan Promjeen Suphat Phongthai Kanjana Singh Worrapob Chaisan Peeraporn Pakakaew Somdet Srichairatanakool Rajnibhas Sukeaw Samakradhamrongthai Niramon Utama-ang |
| author_facet | Kanokwan Promjeen Suphat Phongthai Kanjana Singh Worrapob Chaisan Peeraporn Pakakaew Somdet Srichairatanakool Rajnibhas Sukeaw Samakradhamrongthai Niramon Utama-ang |
| author_sort | Kanokwan Promjeen |
| collection | DOAJ |
| description | Mung bean is a rich protein source, but its native form has limited solubility and functionality for food applications. As a promising agro-based crop, mung bean offers a sustainable alternative to traditional protein sources, especially in regions with limited access to resources. This study optimized mung bean protein hydrolysate (MBPH) production using response surface methodology (RSM), investigating the effects of alcalase concentration (2–7%) and hydrolysis time (2–7 h) on its physicochemical and functional properties. The results showed that an alcalase concentration of 5.88% and a hydrolysis duration of 3.56 h were the optimal conditions, resulting in a degree of hydrolysis of approximately 33.09%. Under these conditions, MBPH contained 79.33 ± 0.62% protein and a molecular weight distribution of 45.57% and 47.29% at 1.1–10 kDa and <10 kDa, respectively. Additionally, MBPH exhibited strong antioxidant activity, improved foam capacity, and enhanced solubility, making it a valuable ingredient for sustainable food production and promoting equitable access to nutritious functional ingredients. |
| format | Article |
| id | doaj-art-591a5dc747b6473da0e4f08bf291401f |
| institution | Kabale University |
| issn | 2304-8158 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj-art-591a5dc747b6473da0e4f08bf291401f2025-08-20T03:35:28ZengMDPI AGFoods2304-81582025-07-011414245910.3390/foods14142459Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional PropertiesKanokwan Promjeen0Suphat Phongthai1Kanjana Singh2Worrapob Chaisan3Peeraporn Pakakaew4Somdet Srichairatanakool5Rajnibhas Sukeaw Samakradhamrongthai6Niramon Utama-ang7Division of Product Development Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandDivision of Food Science and Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandDivision of Product Development Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandCluster of High Value Products from Thai Rice and Plants for Health, Chiang Mai University, Chiang Mai 50100, ThailandDivision of Food Science and Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, ThailandDivision of Product Development Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandDivision of Product Development Technology, Faculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, ThailandMung bean is a rich protein source, but its native form has limited solubility and functionality for food applications. As a promising agro-based crop, mung bean offers a sustainable alternative to traditional protein sources, especially in regions with limited access to resources. This study optimized mung bean protein hydrolysate (MBPH) production using response surface methodology (RSM), investigating the effects of alcalase concentration (2–7%) and hydrolysis time (2–7 h) on its physicochemical and functional properties. The results showed that an alcalase concentration of 5.88% and a hydrolysis duration of 3.56 h were the optimal conditions, resulting in a degree of hydrolysis of approximately 33.09%. Under these conditions, MBPH contained 79.33 ± 0.62% protein and a molecular weight distribution of 45.57% and 47.29% at 1.1–10 kDa and <10 kDa, respectively. Additionally, MBPH exhibited strong antioxidant activity, improved foam capacity, and enhanced solubility, making it a valuable ingredient for sustainable food production and promoting equitable access to nutritious functional ingredients.https://www.mdpi.com/2304-8158/14/14/2459mung beanprotein hydrolysatemung bean peptidesfunctional propertiesalcalase enzymeoptimization |
| spellingShingle | Kanokwan Promjeen Suphat Phongthai Kanjana Singh Worrapob Chaisan Peeraporn Pakakaew Somdet Srichairatanakool Rajnibhas Sukeaw Samakradhamrongthai Niramon Utama-ang Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties Foods mung bean protein hydrolysate mung bean peptides functional properties alcalase enzyme optimization |
| title | Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties |
| title_full | Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties |
| title_fullStr | Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties |
| title_full_unstemmed | Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties |
| title_short | Optimization of Enzymatic Protein Hydrolysate from Mung Bean (<i>Vigna radiata</i> L.), and Its Functional Properties |
| title_sort | optimization of enzymatic protein hydrolysate from mung bean i vigna radiata i l and its functional properties |
| topic | mung bean protein hydrolysate mung bean peptides functional properties alcalase enzyme optimization |
| url | https://www.mdpi.com/2304-8158/14/14/2459 |
| work_keys_str_mv | AT kanokwanpromjeen optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT suphatphongthai optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT kanjanasingh optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT worrapobchaisan optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT peerapornpakakaew optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT somdetsrichairatanakool optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT rajnibhassukeawsamakradhamrongthai optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties AT niramonutamaang optimizationofenzymaticproteinhydrolysatefrommungbeanivignaradiatailanditsfunctionalproperties |