Functional properties of yam bean (Pachyrhizus erosus) starch

2003 ◽  
Vol 89 (1) ◽  
pp. 103-106 ◽  
Author(s):  
E Mélo
2017 ◽  
Vol 6 (2) ◽  
pp. 457-463 ◽  
Author(s):  
Evelyn S. Buckman ◽  
Ibok Oduro ◽  
Wisdom A. Plahar ◽  
Charles Tortoe

2020 ◽  
Vol 26 (1) ◽  
pp. 159-166
Author(s):  
Fadli Hafizulhaq ◽  
Hairul Abral ◽  
Anwar Kasim ◽  
Syukri Arief

2014 ◽  
Vol 3 (6) ◽  
pp. 168
Author(s):  
Abbas Kisambira ◽  
John H. Muyonga ◽  
Yusuf B. Byaruhanga ◽  
Phinehas Tukamuhabwa ◽  
Silver Tumwegamire ◽  
...  

<p>This study sought to determine the physicochemical and functional properties of yam bean (<em>Pachyrhizus erosus</em>) seed proteins. <em>Pachyrhizus erosus</em> seeds from two accessions (UYB 06 and UYB 07) were milled into flours and then defatted. A portion of the defatted flour was used for production of protein isolates and protein fractions. The physicochemical and functional properties, <em>in vitro</em> digestibility and electrophoretic pattern of the flour and protein isolate were determined. The results showed that albumins (53.3%) were the dominant protein fraction followed by globulins (18.7%), glutelins (8.8%) and prolamins (2.7%). Regarding functional properties, the <em>Pachyrhizus erosus</em> seed protein isolates exhibited 8% of least gelation concentration, water absorption capacity of 3.0 g g<sup>-1</sup>, oil absorption capacity of 0.8 g g<sup>-1</sup>, protein solubility of 81.0%, foaming capacity of 37.1%, foam stability of 73.8%, emulsion activity of 13.8% and emulsion stability of 9.2%. <em>In vitro</em> protein digestibility of the raw and cooked beans was 87.6% and 84.3%, respectively. The electrophoretic pattern of<em> Pachyrhizus erosus</em> protein showed major bands corresponding to molecular weight 13.3, 15, 29.8, 54.4 and above 84.7 kDa. The results, suggest that <em>Pachyrhizus erosus </em>seed protein has potential for use in both food and non-food applications such as films and coating.</p>


Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.


2001 ◽  
Vol 268 (6) ◽  
pp. 1739-1748
Author(s):  
Aitor Hierro ◽  
Jesus M. Arizmendi ◽  
Javier De Las Rivas ◽  
M. Angeles Urbaneja ◽  
Adelina Prado ◽  
...  

Author(s):  
Anna Pomés ◽  
Alisa Smith ◽  
Christophe Grégoire ◽  
Lisa Vailes ◽  
L. Arruda ◽  
...  

2016 ◽  
Author(s):  
Ana Feregrino-Perez ◽  
Sandra Jimenez-Garcia ◽  
Moises Vazquez-Cruz ◽  
Laura Mejia-Teniente ◽  
Ramon Guevara-Gonzalez ◽  
...  

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