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Techno-functional properties and allergenicity of mung bean (Vigna radiata) protein isolates from Imara and KPS2 varieties.
Chin, Tak Gun Jeremy; Ruethers, Thimo; Chan, Bing Aleo; Lopata, Andreas Ludwig; Du, Juan.
Affiliation
  • Chin TGJ; Food, Chemical and Biotechnology Cluster, Singapore Institute of Technology, 10 Dover Drive, Singapore 138683, Singapore.
  • Ruethers T; Tropical Futures Institute, James Cook University Singapore, 149 Sims Drive, Singapore 387380, Singapore; Molecular Allergy Research Laboratory, College of Public Health, Medical and Veterinary Sciences, Australian Institute of Tropical Health and Medicine, James Cook University, 1 James Cook Drive,
  • Chan BA; Food, Chemical and Biotechnology Cluster, Singapore Institute of Technology, 10 Dover Drive, Singapore 138683, Singapore.
  • Lopata AL; Tropical Futures Institute, James Cook University Singapore, 149 Sims Drive, Singapore 387380, Singapore; Molecular Allergy Research Laboratory, College of Public Health, Medical and Veterinary Sciences, Australian Institute of Tropical Health and Medicine, James Cook University, 1 James Cook Drive,
  • Du J; Food, Chemical and Biotechnology Cluster, Singapore Institute of Technology, 10 Dover Drive, Singapore 138683, Singapore; Department of Food Science, Purdue University, 745 Agriculture Mall Dr, West Lafayette, IN 47907, USA; Sengkang General Hospital, Singapore Health Services, 10 Hospital Boulevard
Food Chem ; 457: 140069, 2024 Nov 01.
Article de En | MEDLINE | ID: mdl-38936132
ABSTRACT
Mung bean is an increasingly cultivated legume. This study compared mung bean varieties 'KPS2' from Thailand (Th) and 'Imara' from Tanzania (T) with a focus on protein composition, allergenicity, and techno-functional properties. Two rounds alkaline-acid extraction were performed to produce mung bean protein isolate (MBPI - Th1/T1 and Th2/T2), supernatant (S) and protein-poor residue (PPR). Mass spectrometric analysis revealed high abundance of 8 s-vicilin and 11 s-legumin in MBPI and S. Extraction removed considerable amounts of the seed albumin allergen but increased the relative abundance of cupins in MBPI. Higher vicilin levels were found in Th1 samples, contributed to increased protein solubility above pH 6.5. Th formed stronger gels which were more stable at higher frequencies. In contrast, T proteins were structurally more flexible, leading to its improved foaming ability. This study provides the knowledge and methods for appropriate selection of mung bean varieties for various food applications.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Protéines végétales / Allergènes / Vigna Limites: Humans Pays/Région comme sujet: Africa / Asia Langue: En Journal: Food Chem / Food chem / Food chemistry Année: 2024 Type de document: Article Pays d'affiliation: Singapour Pays de publication: Royaume-Uni

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Protéines végétales / Allergènes / Vigna Limites: Humans Pays/Région comme sujet: Africa / Asia Langue: En Journal: Food Chem / Food chem / Food chemistry Année: 2024 Type de document: Article Pays d'affiliation: Singapour Pays de publication: Royaume-Uni