Role of the bolus degree of structure on the protein digestibility during in vitro digestion of a pea protein‐fortified sponge cake chewed by elderly

Author(s):  
Melissa Assad‐Bustillos ◽  
Juliette Palier ◽  
Hanitra Rabesona ◽  
Yvan Choiset ◽  
Guy Della Valle ◽  
...  
2020 ◽  
Vol 11 (9) ◽  
pp. 7611-7625
Author(s):  
Kulwa F. Miraji ◽  
Anita R. Linnemann ◽  
Vincenzo Fogliano ◽  
Henry S. Laswai ◽  
Edoardo Capuano

The nutritional contents of rice decreased as grains matured, and pepeta-type processing improves the nutritional properties and in vitro protein digestibility of rice.


2010 ◽  
Vol 24 (8) ◽  
pp. 719-725 ◽  
Author(s):  
Min Hu ◽  
Yan Li ◽  
Eric Andrew Decker ◽  
David Julian McClements

2014 ◽  
Vol 7 ◽  
pp. 1-8 ◽  
Author(s):  
Ashok Kumar Shrestha

Recent advances have shown that differences in compositional, structural and physical properties of caseins and whey proteins affect their digestion and absorption behavior, hormonal response, satiety effect and other physiological effects. For example, the ingestion of whey protein cause fast, high and transient increase of amino acids ‘fast protein’, whereas casein induce slower, lower and prolonged increase of ‘slow protein’ in the gut. Knowledge of, and control over, the rate and nature of digestive breakdown of dairy proteins provides a potential basis for product/process innovation through identifying ingredients and formulations that provide desired nutrient delivery profiles. With this background, the aim of our current review paper is to understand the digestion behavior of various protein-rich milk powders and their potential use in formulation of dairy foods for controlled release of amino acids and energy. Currently available in vitro protein digestibility methods to measure or predict the dairy protein digestibility were also investigated. The author has also presented the preliminary results of ongoing study on in vitro digestion of various commercial proteins powders.DOI: http://dx.doi.org/10.3126/jfstn.v7i0.10560 J. Food Sci. Technol. Nepal, Vol. 7 (1-8), 2012


2013 ◽  
Vol 96 (7) ◽  
pp. 4258-4268 ◽  
Author(s):  
Solène Le Maux ◽  
André Brodkorb ◽  
Thomas Croguennec ◽  
Alan A. Hennessy ◽  
Saïd Bouhallab ◽  
...  

Meat Science ◽  
2020 ◽  
Vol 169 ◽  
pp. 108210 ◽  
Author(s):  
Seonmin Lee ◽  
Kyung Jo ◽  
Hyun Jung Lee ◽  
Cheorun Jo ◽  
Hae In Yong ◽  
...  

2016 ◽  
Vol 11 (8) ◽  
pp. 1934578X1601100 ◽  
Author(s):  
Wojciech Koch ◽  
Wirginia Kukula-Koch ◽  
Marcin Dziedzic ◽  
Kazimierz Głowniak ◽  
Yoshinori Asakawa

Zingiber officinale (Zingiberaceae) is a common spice and a medicine widely cultivated in tropical and subtropical climate around the globe, which contains both precious polyphenols and terpenes in its extracts. The ubiquity of ginger in a variety of foods encouraged the authors to assess the influence of thermal processing and digestion of the plant material on its antioxidant capacity. The obtained results of DPPH assay showed marked differences in the antioxidant potential of the processed samples, in comparison with fresh ginger rhizomes. Autoclave and microwave heating procedures were found to evoke the mildest decomposition of the antioxidants and increase the antioxidant capacity of the plant (from IC50 of 210±10 for a fresh rhizome to ca 160±16 μg/mL for the former, and to 150±18 for the latter technique), whereas frying and boiling for different durations significantly deteriorated the antiradical potential up to IC50 = 940±36 μg/mL. Mouth and stomach digestion decreased the antioxidant potential of the extracts even to ca. 1000±47 μg/mL. A protective role of saliva towards the antioxidant compounds against hydrochloric acid and pepsin activities has been proven. A marked deterioration in antioxidant capacity in digested rhizomes may shed new light on the actual absorption of consumed polyphenols with food products.


2019 ◽  
Vol 279 ◽  
pp. 252-259 ◽  
Author(s):  
Sergio Pérez-Burillo ◽  
Trupthi Mehta ◽  
Adelaida Esteban-Muñoz ◽  
Silvia Pastoriza ◽  
Oleg Paliy ◽  
...  

1982 ◽  
Vol 62 (2) ◽  
pp. 657-660 ◽  
Author(s):  
B. E. MARCH ◽  
D. R. HICKLING

A control fish meal and an overheated fish meal were compared by in vitro digestion with pepsin at concentrations of 10−5 to 10−1 and at temperatures from 10 to 40 °C. The reduction in protein solubilization caused by over-heating was most evident with pepsin digestion at 10 and 20 °C and suggests modification of the standard method when evaluating fish meals to be fed to cold-water fish. Key words: Protein digestibility, pepsin digestibility, fish meal, cold-water fish


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