Pheasant Egg White Lysozyme vs. Hen Egg White Lysozyme: A Comparative Study of Enzymatic Activity

Pheasant Egg White Lysozyme vs. Hen Egg White Lysozyme: A Comparative Study of Enzymatic Activity Full article

Journal

Foods
ISSN: 2304-8158

Output data

Year: 2026, Volume: 15, Number: 19, Article number : 3402, Pages count : DOI: 10.3390/foods15193402

Authors

Mukhametova Liliya I. ¹ , Zherdev Dmitry O. ^1,2 , Kuznetsov Anton N. ³ , Burykina Julia V. ⁴ , Yudina Olga N. ² , Filimonova Svetlana M. ⁵ , Eremin Sergei A. ¹ , Krylov Vadim B. ³ , Nifantiev Nikolay E. ²

Affiliations

1	Faculty of Chemistry, M.V. Lomonosov Moscow State University, Leninsky Gory 1/3, 119991 Moscow, Russia
2	Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, 119991 Moscow, Russia
3	Laboratory of Synthetic Glycovaccines, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, 119991 Moscow, Russia
4	Laboratory of Metal-Complex and Nanoscale Catalysts, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, 119991 Moscow, Russia
5	Institute of Pharmacy, FSAEI HE I.M. Sechenov First MSMU of MOH of Russia (Sechenovskiy University), 119435 Moscow, Russia

Hen egg white lysozyme (HEWL) is a well-characterized antibacterial enzyme widely used in research and industry. However, little is known about the functional properties of lysozyme from other bird species, such as pheasants. This study aimed to compare the muramidase and chitinase activities of HEWL with the lysozyme from pheasant egg white (PEWL). Egg white samples were obtained from ten hens and ten pheasants. Lysozyme activity was assessed by two methods: a turbidimetric assay using Micrococcus luteus cell suspension to measure bacteriolytic (muramidase) activity and a fluorescence polarization assay (FPA) using FITC-labeled tri- and chitopentaoside substrates to measure the chitinase activity. The observed dissociation rate constant (kobs) was derived from the time-dependent FP signal. Turbidimetric measurements showed that PEWL possessed bacteriolytic activity approximately 30% lower than that of HEWL under the same conditions. However, FPA revealed a striking functional difference: whereas HEWL only bound the chitotrioside substrate without hydrolyzing it, PEWL was able to hydrolyze chitotriose. Both enzymes readily hydrolyzed the chitopentaoside substrate. The hydrolysis rate of the chitopentaoside was 50–70 times higher than that of the chitotrioside for PEWL. Sequence comparison identified six amino acid substitutions in PEWL (Phe3 → Tyr, His15 → Leu, Gln41 → His, Asn77 → His, Gln121 → Asn, Ile124 → Thr) relative to HEWL, which likely alter the conformation of subsites A–C and enable productive binding of the shorter oligosaccharide. Thus, despite high sequence similarity, pheasant lysozyme exhibits a unique functional property—the ability to hydrolyze chitotriose into N-acetylglucosamine. These findings expand functions of avian lysozymes and highlight the potential of alternative bird species as sources of enzymes with novel properties.

Mukhametova L.I. , Zherdev D.O. , Kuznetsov A.N. , Burykina J.V. , Yudina O.N. , Filimonova S.M. , Eremin S.A. , Krylov V.B. , Nifantiev N.E.
Pheasant Egg White Lysozyme vs. Hen Egg White Lysozyme: A Comparative Study of Enzymatic Activity
Foods. 2026. V.15. N19. 3402 . DOI: 10.3390/foods15193402 WOS Scopus OpenAlex

Submitted:	Jul 13, 2026
Published online:	Sep 24, 2026

≡ Web of science:	WOS:001902784800001
≡ Scopus:	2-s2.0-105053618802
≡ OpenAlex:	W7214192117