Comparative biochemistry of penguin egg- white proteins—I. ovomucoids: Composition and inhibitory activities for trypsin, α-chymotrypsin and subtilisin

1974 ◽  
Vol 48 (4) ◽  
pp. 519-533 ◽  
Author(s):  
David T. Osuga ◽  
John C. Bigler ◽  
Ruth L. Uy ◽  
Lars Sjöberg ◽  
Robert E. Feeney
Keyword(s):  
Egg White ◽  
Comparative Biochemistry ◽  
Egg White Proteins ◽  
Inhibitory Activities

scholarly journals Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides

Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1312
Author(s):  
Pei-Gee Yap ◽  
Chee-Yuen Gan
Keyword(s):  
Bioactive Peptides ◽  
Egg White ◽  
Degree Of Hydrolysis ◽  
Hydrolysis Time ◽  
Relationship Analysis ◽  
Activity Inhibition ◽  
Chicken Egg ◽  
Egg White Proteins ◽  
Inhibitory Activities ◽  
Active Fragments

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy.

scholarly journals The Comparative Biochemistry of Avian Egg White Proteins

1960 ◽  
Vol 235 (8) ◽  
pp. 2307-2311 ◽  
Author(s):  
Robert E. Feeney ◽  
John S. Anderson ◽  
Parviz R. Azari ◽  
Nelle Bennett ◽  
Marvin B. Rhodes
Keyword(s):  
Egg White ◽  
Comparative Biochemistry ◽  
Egg White Proteins ◽  
Avian Egg

Identification of Egg White Proteins and Divergence in the Regulatory Region of the Ovalbumin Gene in Avians

2016 ◽  
Vol 24 (1) ◽  
pp. 12-25 ◽  
Author(s):  
Jindong Ren ◽  
Jianhong Hu ◽  
Li Chen ◽  
Yali Liu ◽  
Xiaoqin Xu ◽  
...  
Keyword(s):  
Regulatory Region ◽  
Egg White ◽  
Egg White Proteins

scholarly journals EGG WHITE PROTEINS

1950 ◽  
Vol 184 (1) ◽  
pp. 377-383 ◽  
Author(s):  
Richard H. Forsythe ◽  
Joseph F. Foster
Keyword(s):  
Egg White ◽  
Egg White Proteins

scholarly journals Magnum Morphogenesis during the Natural Development of the Quail Oviduct: Analysis of Egg White Proteins and Progesterone Receptor Concentration1

1986 ◽  
Vol 35 (3) ◽  
pp. 657-666 ◽  
Author(s):  
J. F. Pageaux ◽  
C. Laugier ◽  
D. Pal ◽  
M. A. D’Almeida ◽  
D. Sandoz ◽  
...  
Keyword(s):  
Progesterone Receptor ◽  
Egg White ◽  
Natural Development ◽  
Egg White Proteins

Peptic digestibility of raw and heat-coagulated hen's egg white proteins at acidic pH range

2004 ◽  
Vol 55 (8) ◽  
pp. 635-640 ◽  
Author(s):  
Kenji Yoshino ◽  
Kentaro Sakai ◽  
Yoko Mizuha ◽  
Ayako Shimizuike ◽  
Shigeru Yamamoto
Keyword(s):  
Egg White ◽  
Acidic Ph ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Ph Range
Sign in / Sign up

Export Citation Format

Share Document