This study took the liver ferritin of the Baerii sturgeon (Acipenser baerii), Schrencki sturgeon (Acipenser schrenckii) and hybrid sturgeon (Huso huso).The isolated ferritins were designated as SLF-1, SLF-2, and SLF-3, respectively.To investigate the structural and physicochemical properties of these three sturgeon liver ferritins, this study employed a systematic approach utilizing various methods, including electrophoresis, transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FTIR), and amino acid composition analysis.Furthermore, a bioinformatics analysis was performed to compare the similarities and differences among the three sturgeon liver ferritins.The transmission electron microscopy (TEM) images revealed that SLF-1, SLF-2, and SLF-3 all exhibited a spherical morphology with a uniform particle size distribution, characterized by an outer diameter of approximately 12 nm.Additionally, Fourier transform infrared spectroscopy (FTIR) analysis indicated that the overall secondary structures of the three ferritins were comparable;however, it was noted that the α-helix content of SLF-2 was relatively low, measuring only 52.79%.Additionally, the total amino acid content of all three ferritins exceeded 600 mg/g, with SLF-1 exhibiting the highest content and SLF-3 the lowest.Bioinformatics analysis indicated that SLF-1, SLF-2, and SLF-3 were hydrophilic proteins, classified as non-secretory proteins.Each of these ferritins possessed a subunit structure comprising four antiparallel α-helices, which played crucial roles in maintaining protein structural stability and iron balance within organisms.This study provides a significant theoretical foundation for understanding the functional characteristics of sturgeon liver ferritins.
SHEN Miaomiao
,
YUAN Bo
,
ZHANG Yujie
,
LI Meizhu
,
TAO Tongxi
,
LI Shuhong
,
LI Ran
,
ZHOU Man
,
ZHANG Zhiqing
,
LI Meiliang
. Comparative study of structure and physicochemical characteristics of liver ferritin from three sturgeon species[J]. Food and Fermentation Industries, 2025
, 51(22)
: 189
-197
.
DOI: 10.13995/j.cnki.11-1802/ts.042548
[1] CHEN H, HAN X E, FU Y, et al.Compartmentalized chitooligosaccharide/ferritin particles for controlled co-encapsulation of curcumin and rutin[J].Carbohydrate Polymers, 2022, 290:119484.
[2] BOU-ABDALLAH F, FISH J, TERASHI G, et al.Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism[J].Protein Science, 2024, 33(8):e5104.
[3] SONG Z Y, NI W J, LI B Z,et al.Sustainable ferritin from bovine by-product liver as a potential resource:Ultrasound assisted extraction and physicochemical, structural, functional, and stable analysis[J].International Journal of Biological Macromolecules, 2024, 281:136264.
[4] CHAKRABORTI S, CHAKRABARTI P.Self-assembly of ferritin:Structure, biological function and potential applications in nanotechnology[J].Advances in Experimental Medicine and Biology, 2019, 1174:313-329.
[5] CHEN R, LIU Z, WANG J Z, et al.A review of the nutritional value and biological activities of sturgeon processed byproducts[J].Frontiers in Nutrition, 2022, 9:1024309.
[6] ZHU L L, LI J W, WANG Y C, et al.Structural feature and self-assembly properties of type Ⅱ collagens from the cartilages of skate and sturgeon[J].Food Chemistry, 2020, 331:127340.
[7] FENG W W, ZHAO T, ZHOU Y, et al.Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin[J].Pharmacognosy Magazine, 2013, 9(Suppl 1):S32-S37.
[8] ZHANG S Y, DENG X R, GUO X, et al.Sustained release of chlorogenic acid by co-encapsulation of sodium alginate binding to the Northern pike (Esox Lucius) liver ferritin[J].Food Chemistry, 2023, 429:136924.
[9] 丁炳文. 鲟鱼肝脏铁蛋白理化特性研究及其载钙复合物制备的初步探究[D].雅安:四川农业大学, 2021.
DING B W.Study on the physicochemical properties of liver ferritin of acipenser baerii and preliminary study on the preparation of ferritin-calcium complex[D].Ya’an:College of Food Science, Sichuan Agricultural University, 2021.
[10] LAEMMLI U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J].Nature, 1970, 227(5259):680-685.
[11] LI H, TAN X Y, XIA X Y, et al.Thermal treatment modified the physicochemical properties of recombinant oyster (Crassostrea gigas) ferritin[J].Food Chemistry, 2020, 314:126210.
[12] 李蝶, 张斌, 申淼淼, 等.基于重组虾铁蛋白装载山奈酚的三种不同方法的比较分析[J].食品与发酵工业, 2023, 49(24):251-258.
LI D, ZHANG B, SHEN M M, et al.Comparative analysis of three different loading methods of kaempferol based on recombinant marsupenaeus japonicus ferritin[J].Food and Fermentation Industries, 2023, 49(24):251-258.
[13] WANG S N, GUO Y H, LIN K, et al.Study on ferritin glycation with dextran:Physicochemical characterization and its application in the delivery of resveratrol[J].LWT, 2024, 205:116498.
[14] YANG C, LIU W Y, ZHU X J, et al.Ultrasound-assisted enzymatic digestion for efficient extraction of proteins from quinoa[J].LWT, 2024, 194:115784.
[15] 夏小雨, 李晗, 王震宇, 等.人源重链铁蛋白纯化及其纳米粒制备[J].食品科学, 2020, 41(12):91-98.
XIA X Y, LI H, WANG Z Y, et al.Purification and preparation of nanoparticles of human H-chain ferritin[J].Food Science, 2020, 41(12):91-98.
[16] 丁炳文, 马贵红, 李筱, 等.热处理对鲟鱼肝脏铁蛋白稳定性的影响[J].食品科学, 2022, 43(8):66-73.
DING B W, MA G H, LI X, et al.Effects of heat treatment on the stability of liver ferritin from Acipenser baerii[J].Food Science, 2022, 43(8):66-73.
[17] YANG R, MA J R, HU J N, et al.Formation of ferritin-agaro oligosaccharide-epigallocatechin gallate nanoparticle induced by CHAPS and partitioned by the ferritin shell with enhanced delivery efficiency[J].Food Hydrocolloids, 2023, 137:108396.
[18] CHANG X X, LV C Y, ZHAO G H.A dual function of ferritin (animal and plant):Its holo form for iron supplementation and apo form for delivery systems[J].Annual Review of Food Science and Technology, 2023, 14:113-133.
[19] CHEN H, TAN X Y, HAN X E, et al.Ferritin nanocage based delivery vehicles:From single-, co- to compartmentalized- encapsulation of bioactive or nutraceutical compounds[J].Biotechnology Advances, 2022, 61:108037.
[20] YANG R, LIU Y Q, GAO Y J, et al.Ferritin glycosylated by chitosan as a novel EGCG nano-carrier:Structure, stability, and absorption analysis[J].International Journal of Biological Macromolecules, 2017, 105:252-261.
[21] LI Y W, LI B.Characterization of structure-antioxidant activity relationship of peptides in free radical systems using QSAR models:Key sequence positions and their amino acid properties[J].Journal of Theoretical Biology, 2013, 318:29-43.
[22] INSANG S, KIJPATANASILP I, JAFARI S, et al.Ultrasound assisted extraction of functional compound from mulberry (Morus alba L.) leaf using response surface methodology and effect of microencapsulation by spray drying on quality of optimized extract[J].Ultrasonics Sonochemistry, 2022, 82:105806.
[23] TRAN N T, LIU H, JAKOVLIĆI, et al.Blunt snout bream (Megalobrama amblycephala) MyD88 and TRAF6:Characterisation, comparative homology modelling and expression[J].International Journal of Molecular Sciences, 2015;16(4):7077-7097.
[24] WANG F, XU W Q, ZHANG W Q, et al. Transferrin receptor 1 promotes hepatocellular carcinoma progression and metastasis by activating the mTOR signaling pathway[J].Hepatology International, 2024, 18(2):636-650.
[25] XU Y, LI Y T, LI J X, et al.Ethyl carbamate triggers ferroptosis in liver through inhibiting GSH synthesis and suppressing Nrf2 activation[J].Redox Biology, 2022, 53:102349.
