Enzymatic Hydrolysis of Chicken Viscera to Obtain Added-Value Protein Hydrolysates with Antioxidant and Antihypertensive Properties

2019 ◽  
Vol 26 (2) ◽  
pp. 717-725 ◽  
Author(s):  
Jessika Gonçalves dos Santos Aguilar ◽  
Ana Karoliny Santos de Souza ◽  
Ruann Janser Soares de Castro
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.  


Fermentation ◽  
2020 ◽  
Vol 6 (1) ◽  
pp. 31
Author(s):  
María Emilia Cano ◽  
Alberto García-Martin ◽  
Pablo Comendador Morales ◽  
Mateusz Wojtusik ◽  
Victoria E. Santos ◽  
...  

The development of biorefinery processes to platform chemicals for most lignocellulosic substrates, results in side processes to intermediates such as oligosaccharides. Agrofood wastes are most amenable to produce such intermediates, in particular, cellooligo-saccharides (COS), pectooligosaccharides (POS), xylooligosaccharides (XOS) and other less abundant oligomers containing mannose, arabinose, galactose and several sugar acids. These compounds show a remarkable bioactivity as prebiotics, elicitors in plants, food complements, healthy coadyuvants in certain therapies and more. They are medium to high added-value compounds with an increasing impact in the pharmaceutical, nutraceutical, cosmetic and food industries. This review is focused on the main production processes: autohydrolysis, acid and basic catalysis and enzymatic saccharification. Autohydrolysis of food residues at 160–190 °C leads to oligomer yields in the 0.06–0.3 g/g dry solid range, while acid hydrolysis of pectin (80–120 °C) or cellulose (45–180 °C) yields up to 0.7 g/g dry polymer. Enzymatic hydrolysis at 40–50 °C of pure polysaccharides results in 0.06–0.35 g/g dry solid (DS), with values in the range 0.08–0.2 g/g DS for original food residues.


2009 ◽  
Vol 45 (6) ◽  
pp. 648-655 ◽  
Author(s):  
N. L. Eremeev ◽  
I. V. Nikolaev ◽  
I. D. Keruchen’ko ◽  
E. V. Stepanova ◽  
A. D. Satrutdinov ◽  
...  

2018 ◽  
Vol 9 (1) ◽  
pp. 407-416 ◽  
Author(s):  
Alice B. Nongonierma ◽  
Candice Lamoureux ◽  
Richard J. FitzGerald

Cricket (Gryllodes sigillatus) protein hydrolysates inhibit dipeptidyl peptidase IV (DPP-IV) in vitro.


2018 ◽  
Vol 76 ◽  
pp. 103-112 ◽  
Author(s):  
Pattraporn Sukkhown ◽  
Kamolwan Jangchud ◽  
Yaowapa Lorjaroenphon ◽  
Tantawan Pirak

LWT ◽  
2011 ◽  
Vol 44 (2) ◽  
pp. 421-428 ◽  
Author(s):  
Hu Hou ◽  
Bafang Li ◽  
Xue Zhao ◽  
Zhaohui Zhang ◽  
Pinglin Li

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