Some functional properties of peanut proteins partially hydrolyzed with papain

1978 ◽  
Vol 26 (4) ◽  
pp. 855-858 ◽  
Author(s):  
Antonio A. Sekul ◽  
Carolyn H. Vinnett ◽  
Robert L. Ory
2021 ◽  
Author(s):  
Apekshita Singh ◽  
Soom Nath Raina ◽  
Manisha Sharma ◽  
Manju Chaudhary ◽  
Suman Sharma ◽  
...  

Peanut (Arachis hypogaea L.) is an important grain legume crop of tropics and subtropics. It is increasingly being accepted as a functional food and protein extender in developing countries. The seed contains 36% to 54% oil, 16% to 36% protein, and 10% to 20% carbohydrates with high amounts of P, Mg, Ca, riboflavin, niacin, folic acid, vitamin E, resveratrol and amino acids. Seed contains 32 different proteins comprised of albumins and globulins. The two-globulin fractions, arachin and non-arachin, comprise approximately 87% of the peanut seed proteins. Peanut worldwide is mainly used for oil production, consumption as raw, roasted, baked products, peanut butter, peanut flour, extender in meat product formulations, confectionary and soups. Peanut proteins have many properties such as good solubility, foaming, water/oil binding, emulsification that make them useful in various food products. Very limited studies have been carried out in peanut functional properties, which has been reviewed in the present article. Adequate modifications can be done in protein functionality that are influenced by pH, temperature, pressure etc. However, some individuals develop severe IgE-mediated allergies to peanut seed proteins. Thus, methods to improve nutrition and reduce allergenicity have also been discussed. Within the last decade, manipulations have been done to alter peanut chemistry and improve nutritional quality of peanuts and peanut products. Hence, improved comprehensive understanding of functional properties and nutritional chemistry of peanut proteins can generate better source of food grain to meet nutritional requirement of growing population. In the present review, composition of peanut seed proteins, functional properties, nutritional components and nutraceutical value have been discussed with respect to beneficial aspects to health, reducing hunger and usage in food end products.


2015 ◽  
Vol 1090 ◽  
pp. 117-122
Author(s):  
Yue Shao ◽  
Xiang Long Liu ◽  
Hong Shao ◽  
Yun Jiao Li

The functional properties of peanut protein were determined under different conditions of ultrasonic waves which are used for processing the solution of peanut protein powder. The functional properties of peanut protein were enhanced remarkably by ultrasonic waves. Processed by ultrasonic waves for20 min, foaming ability increases to 60% from 30%, and foam stability increases to 50% from 17%. Processed by ultrasonic waves for 15 min, emulsifying ability increases to 49.3% from 38.9% obviously, and emulsion stability increases to 100% from 91.4%.When the solution’s PH equals 4, foaming ability of peanut protein to be minimum. Foaming ability increases to 27.9% from 26.2% by ultrasonic waves. When the solution’s PH is from 6 to 10, emulsifying ability increases to 50.7% from 44.3% by ultrasonic waves. When the concentration of the solution of NaCl is 0.2mol/L~0.4mol/L, emulsifying ability increases to 45% from 38.4% by ultrasonic waves, but it will drop if we continue to increase the concentration of the solution of NaCl. Processed by ultrasonic waves for 6 min,oil absorption ability increases to 1.51 mL/g from 1.26 mL/g. Processed by ultrasonic waves for 8 min, the solubility of low concentration peanut protein solution (1g /100mL~2g/100mL) enhanced doubly, and the water holding capacity increases to 2.9% from 2.4%.


2019 ◽  
Vol 97 (1) ◽  
pp. 93-103 ◽  
Author(s):  
Shao Bing Zhang ◽  
Xiao Hua Wang ◽  
Xia Li ◽  
Dong Qiong Yan

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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