Antioxidant activities and functional properties of tea seed protein hydrolysates (Camellia oleifera Abel.) influenced by the degree of enzymatic hydrolysis

2014 ◽  
Vol 23 (6) ◽  
pp. 2075-2082 ◽  
Author(s):  
Xu Li ◽  
Shian Shen ◽  
Junlin Deng ◽  
Tian Li ◽  
Chunbang Ding
Author(s):  
Vitor Geniselli da Silva ◽  
Ruann Janser Soares de Castro

Aiming to explore the use of ionic liquids (ILs) not yet described in the literature, this work evaluated the hydrolysis of proteins from chicken viscera using the protease Alcalase modified and unmodified by the IL tetramethylammonium bromide. The protein hydrolysates produced in the presence of the IL presented values of antioxidant activities 40% higher than the hydrolysates obtained without IL. In addition, with the presence of the IL, it was possible to obtain protein hydrolysates from chicken viscera with similar antioxidant activities, compared to the protein hydrolysates produced without IL, using 1/3 of the amount of enzyme.


2011 ◽  
Vol 20 (No. 1) ◽  
pp. 7-14 ◽  
Author(s):  
M. Hrčková ◽  
M. Rusňáková ◽  
J. Zemanovič

Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  


Foods ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 381 ◽  
Author(s):  
Giulia Leni ◽  
Lise Soetemans ◽  
Augusta Caligiani ◽  
Stefano Sforza ◽  
Leen Bastiaens

Protein hydrolysates from lesser mealworm (Alphitobius diaperinus, LM) were obtained by enzymatic hydrolysis with protease from Bacillus licheniformis. A preliminary test performed for five hours of hydrolysis generated an insect protein hydrolysate with 15% of degree of hydrolysis (DH), optimum solubility property and oil holding capacity, but emulsifying and foaming ability were completely impaired. In order to investigate the potential implication of DH on techno-functional properties, a set of protein hydrolysates with a different DH was obtained by sub-sampling at different time points during three hours of enzymatic hydrolysis process. An increase in DH% had positive effects on the solubility property and oil holding ability, while a reduced emulsifying ability was observed up to five hours of hydrolysis. These results demonstrated that the enzymatic hydrolysis, if performed under controlled conditions and not for a long period, represents a valid method to extract high quality protein from insects with tailored techno-functionality, in order to produce tailored ingredients for feed and food purpose.


2012 ◽  
Vol 134 (3) ◽  
pp. 1360-1367 ◽  
Author(s):  
Qiang Zhao ◽  
Hua Xiong ◽  
Cordelia Selomulya ◽  
Xiao Dong Chen ◽  
Honglan Zhong ◽  
...  

Insects ◽  
2020 ◽  
Vol 11 (12) ◽  
pp. 876
Author(s):  
Inayat Batish ◽  
Devon Brits ◽  
Pedro Valencia ◽  
Caio Miyai ◽  
Shamil Rafeeq ◽  
...  

The effects of chemical protein extraction, and enzymatic hydrolysis with Alcalase, papain and pepsin, on the functional properties, antioxidant activity, amino acid composition and protein structure of black soldier fly (H. illucens) larval protein were examined. Alcalase hydrolysates had the highest degree of hydrolysis (p < 0.05), with the highest hydrolysate and oil fraction yield (p < 0.05). Pepsin hydrolysates showed the lowest oil holding capacity (p < 0.05), whereas no significant differences were observed among other enzymes and protein concentrates (p > 0.05). The emulsifying stability and foam capacity were significantly lower in protein hydrolysates than protein concentrate (p < 0.05). The antioxidant activity of protein hydrolysates from protein concentrate and Alcalase was higher than that with papain and pepsin (p < 0.05), owing to the higher hydrophobic amino acid content. Raman spectroscopy indicated structural changes in protein α-helices and β-sheets after enzymatic hydrolysis.


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