Antioxidant and antidiabetic activities of peptides isolated from a hydrolysate of an egg-yolk protein by-product prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia)

RSC Advances ◽  
2015 ◽  
Vol 5 (14) ◽  
pp. 10460-10467 ◽  
Author(s):  
Aleksandra Zambrowicz ◽  
Ewelina Eckert ◽  
Marta Pokora ◽  
Łukasz Bobak ◽  
Anna Dąbrowska ◽  
...  

Peptides isolated from egg yolk protein by-product hydrolysate prepared with unconventional proteinase from Cucurbita ficifolia exert multiple biological activities.

2012 ◽  
Vol 2 (12) ◽  
pp. 487 ◽  
Author(s):  
Aleksandra Zambrowicz ◽  
Marta Pokora ◽  
Ewelina Eckert ◽  
Marek Szołtysik ◽  
Anna Dąbrowska ◽  
...  

Several biological activities have now been associated with egg protein- derived peptides, including antihypertensive, antimicrobial, immunomodulatory, anticancer and antioxidant activities, highlighting the importance of these biopeptides in human health, and disease prevention and treatment. Special attention has been given to peptides with antioxidant and antimicrobial activities as a new source of natural preservatives in food industry. In this study, the antioxidant properties of the egg-yolk protein by-product (YP) hydrolysates were evaluated based on their radical scavenging capacity (DPPH), Fe2+chelating effect and ferric reducing power (FRAP). Furthermore, antimicrobial properties of obtained hydrolysates against Bacillus species were studied. The degrees (DHs) of hydrolysis for 4h hydrolysates were: 19.1%, 13.5% and 13.0%, for pepsin, chymotrypsin and trypsin, respectively. Pepsin was the most effective in producing the free amino groups (1410.3 μmolGly/g). The RP-HPLC profiles of the protein hydrolysates showed differences in the hydrophobicity of the generated peptides. Trypsin hydrolysate obtained after 4h reaction demonstrated the strongest DPPH free radical scavenging activity (0.85 µmol Troloxeq/mg). Trypsin and chymotrypsin hydrolysates obtained after 4h reaction exhibited 4 times higher ferric reducing capacity than those treated by pepsin. The hydrolysis products obtained from YP exhibited significant chelating activity. The 4h trypsin hydrolysate exhibited weak antimicrobial activity against B. subtilis B3; B. cereus B512; B. cereus B 3p and B. laterosporum B6. Keywords: Antioxidative activity, DPPH, peptides, hydrolysis, egg-yolk protei


2014 ◽  
Vol 110 ◽  
pp. 107-116 ◽  
Author(s):  
Ewelina Eckert ◽  
Aleksandra Zambrowicz ◽  
Marta Pokora ◽  
Bartosz Setner ◽  
Anna Dąbrowska ◽  
...  

2008 ◽  
Vol 35 (1) ◽  
pp. 1 ◽  
Author(s):  
Andrew E. Fidler ◽  
Stephen B. Lawrence ◽  
Kenneth P. McNatty

An important goal in the intensive conservation management of New Zealand’s critically endangered nocturnal parrot, kakapo (Strigops habroptilus), is to increase the frequency of breeding attempts. Kakapo breeding does not occur annually but rather correlates with 3–5-year cycles in ‘mast’ seeding/fruiting of kakapo food plants, most notably podocarps such as rimu (Dacrydium cupressinum). Here we advance a hypothetical mechanism for the linking of kakapo breeding with such ‘mast’ seeding/fruiting. The essence of the hypothesis is that exposure to low levels of dietary phytochemicals may, in combination with hepatic gene ‘memory’, sensitise egg yolk protein genes, expressed in female kakapo livers, to oestrogens derived from developing ovarian follicles. Only in those years when the egg yolk protein genes have been sufficiently ‘pre-sensitised’ by dietary chemicals do kakapo ovarian follicles develop to ovulation and egg-laying occurs. While speculative, this hypothesis is both physiologically and evolutionarily plausible and suggests both future research directions and relatively simple interventions that may afford conservation workers some influence over kakapo breeding frequency.


1975 ◽  
Vol 21 (8) ◽  
pp. 1236-1246 ◽  
Author(s):  
W. M. Spira ◽  
J. M. Goepfert

An enterotoxin synthesized during exponential growth by Bacillus cereus produces fluid accumulation in rabbit ileal loops, alters vascular permeability in the skin of rabbits, and kills mice when injected intravenously. All activities are eluted simultaneously from a Sephadex G-75 column and are distinct from the hemolysin and egg yolk turbidity factor of B. cereus. The enterotoxin is a true exotoxin. It interacts with intestinal receptor sites in a highly transient manner in the ileal loop system. Rabbit immune serum produced against the culture fluids from one strain of B. cereus neutralized the three biological activities in all other strains tested except strain B-6-ac for which none of the activities were neutralized.Enterotoxin proved to be unstable under a wide variety of conditions; ionic strength was especially critical. Enterotoxin was most stable in a pH range of 5.0 to 10.0, but lost activity rapidly outside this range. Alkylation provided some protection of enterotoxin activity in crude preparations but failed to protect activity during purification procedures. It did not appear to affect critically the enterotoxin molecule itself, since elution profiles on Sephadex G-75 chromatography were unchanged after alkylation.


1972 ◽  
Vol 55 (5) ◽  
pp. 975-978
Author(s):  
J G Navarro ◽  
F Borie ◽  
J Saavedra

Abstract A residual lipid which is not removed by solvent extraction was detected and determined after enzymatic hydrolysis of defatted egg yolk protein. Free fatty acids were found to be the type of lipid bonded to the egg yolk protein. The mode of attachment of these fatty acids to the egg yolk protein is suggested and the composition of the fatty acids is reported.


LWT ◽  
2020 ◽  
Vol 131 ◽  
pp. 109778
Author(s):  
Chiraz Ben Sassi ◽  
Ismael Marcet ◽  
Manuel Rendueles ◽  
Mario Díaz ◽  
Sami Fattouch

2019 ◽  
Vol 222 (10) ◽  
pp. jeb206185
Author(s):  
Kathryn Knight
Keyword(s):  
Egg Yolk ◽  

2007 ◽  
Vol 13 (4) ◽  
pp. 372-379
Author(s):  
Ryoko KAJINO ◽  
Hiroatsu MATSUOKA ◽  
Kenji SASAGO ◽  
Toshiharu GOMYO
Keyword(s):  
Egg Yolk ◽  

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