Abstract
Oyster protein isolate (OPI) suspensions (6.19 % ± 0.82 %, w/v) were treated by high-pressure homogenization (HPH) at 0 (control), 20, 40, 60, 80 or 100 MPa for three cycles. Protein profiles, secondary structure, free sulfhydryl, surface hydrophobicity, particle size distribution, zeta-potential, solubility, water and oil holding capacity (OHC), emulsifying and foaming properties of the obtained suspensions were analyzed. The results showed that HPH treatment did not cause changes in protein profiles of OPI, but caused changes in secondary structure, content of α-helix decreased but content of β-turn and random coil increased significantly (P < 0.05). Free sulfhydryl and surface hydrophobicity all increased significantly (P < 0.05) after HPH treatment, indicating that tertiary and quaternary structures changed. Functional properties of OPI significantly (P < 0.05) improved after HPH treatment, such as zeta-potential (from −12.67 to −33.57 mV), solubility (from 20.24 % to 57.99 %), OHC (from 981.77 % to 1229.40 %), foaming ability (from 17.50 % to 35.00 %), foaming stability (from 44.49 % to 66.60 %), emulsifying activity index (from 8.87 to 17.06 m2/g) and emulsion stability index (from 14.65 to 41.68 min). At 60 MPa and 80 MPa, the improvements were more remarkable. However, HPH treatment significantly (P < 0.05) decreased particle size (from 200–500 nm to 0–200 nm) and water holding capacity (from 341.15 % to 216.96 %). These improvements were closely related to structural changes and reduction of particle size. Application of different pressures affected functional properties of OPI. These results could provide information for determining HPH applying condition in OPI modification.
Funding statement: This work was supported by the National Natural Science Foundation of China (Grant no. 31771926) and the Basic Research Program of Liaoning Education Department (Grant no. 2016J046).
Conflict of interest: None declared.
References
[1] Ye R, Harte F. High pressure homogenization to improve the stability of casein–hydroxypropyl cellulose aqueous systems. Food Hydrocoll. 2014;35:670–77.10.1016/j.foodhyd.2013.08.022Search in Google Scholar PubMed
[2] Dumay E, Chevalier-Lucia D, Picart-Palmade L, Benzaria A, Gràcia-Julià A, Blayo C. Technological aspects and potential applications of (ultra) high-pressure homogenisation. Trends Food Sci Technol. 2013;31:13–26.10.1016/j.tifs.2012.03.005Search in Google Scholar
[3] Lee S-H, Lefèvre T, Subirade M, Paquin P. Effects of ultra-high pressure homogenization on the properties and structure of interfacial protein layer in whey protein-stabilized emulsion. Food Chem. 2009;113:191–95.10.1016/j.foodchem.2008.07.067Search in Google Scholar
[4] Iordache M, Jelen P. High pressure microfluidization treatment of heat denatured whey proteins for improved functionality. Innov Food Sci Emerg Technol. 2003;4:367–76.10.1016/S1466-8564(03)00061-4Search in Google Scholar
[5] Sun C, Dai L, Liu F, Gao Y. Simultaneous treatment of heat and high pressure homogenization of zein in ethanol–water solution: physical, structural, thermal and morphological characteristics. Innov Food Sci Emerg Tech. 2016;34:161–70.10.1016/j.ifset.2016.01.016Search in Google Scholar
[6] Dong X, Zhao M, Yang BAO, Yang X, Shi J, Jiang Y. Effect of high-pressure homogenization on the functional property of peanut protein. J Food Process Eng. 2011;34:2191–204.10.1111/j.1745-4530.2009.00546.xSearch in Google Scholar
[7] Liu -H-H, Kuo M-I. Ultra high pressure homogenization effect on the proteins in soy flour. Food Hydrocoll. 2016;52:741–48.10.1016/j.foodhyd.2015.08.018Search in Google Scholar
[8] Song X, Zhou C, Fu F, Chen Z, Wu Q. Effect of high-pressure homogenization on particle size and film properties of soy protein isolate. Ind Crops Prod. 2013;43:538–44.10.1016/j.indcrop.2012.08.005Search in Google Scholar
[9] Chen X, Zhou R, Xu X, Zhou G, Liu D. Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder. Food Res Int. 2017;100:193–200.10.1016/j.foodres.2017.07.007Search in Google Scholar PubMed
[10] Grienke U, Silke J, Tasdemir D. Bioactive compounds from marine mussels and their effects on human health. Food Chem. 2014;142:48–60.10.1016/j.foodchem.2013.07.027Search in Google Scholar PubMed
[11] Klomklao S, Kishimura H, Benjakul S. Use of viscera extract from hybrid catfish (Clarias macrocephalus × Clarias gariepinus) for the production of protein hydrolysate from toothed ponyfish (Gazza minuta) muscle. Food Chem. 2013;136:1006–12.10.1016/j.foodchem.2012.09.037Search in Google Scholar PubMed
[12] Wu D, Wu C, Chen H, Wang Z, Yu C, Du M. Effect of ball mill treatment on the physicochemical properties and digestibility of protein extracts generated from scallops (Chlamys farreri). Int J Mol Sci. 2018;19:531.10.3390/ijms19020531Search in Google Scholar
[13] Panozzo A, Manzocco L, Calligaris S, Bartolomeoli I, Maifreni M, Lippe G, et al. Effect of high pressure homogenisation on microbial inactivation, protein structure and functionality of egg white. Food Res Int. 2014;62:718–25.10.1016/j.foodres.2014.04.051Search in Google Scholar
[14] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680–85.10.1038/227680a0Search in Google Scholar PubMed
[15] Hu H, Wu J, Zhu L, Zhang F, Xu X. Effects of ultrasound on structural and physical properties of soy-protein isolate (SPI) dispersions. Food Hydrocoll. 2013;30:647–55.10.1016/j.foodhyd.2012.08.001Search in Google Scholar
[16] Janatova J, Fuller J, Hunter M. The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content. J Biol Chem. 1968;243:3612–22.10.1016/S0021-9258(19)34184-5Search in Google Scholar PubMed
[17] Chelh I, Gatellier P, Santé-Lhoutellier V. Technical note: a simplified procedure for myofibril hydrophobicity determination. Meat Sci. 2006;74:681–83.10.1016/j.meatsci.2006.05.019Search in Google Scholar PubMed
[18] Roy K, Mao H-Q, Huang S-K, Leong KW. Oral gene delivery with chitosan-DNA nanoparticles generates immunologic protection in a murine model of peanut allergy. Nat Med. 1999;5:387–91.10.1038/7385Search in Google Scholar PubMed
[19] Beuchat LR. Functional and electrophoretic characteristics of succinylated peanut flour protein. J Agric Food Chem. 1977;25:258–61.10.1021/jf60210a044Search in Google Scholar
[20] Klompong V, Benjakul S, Kantachote D, Shahidi F. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem. 2007;102:1317–27.10.1016/j.foodchem.2006.07.016Search in Google Scholar
[21] Liceaga-Gesualdo AM, Li-Chan ECY. Functional properties of fish protein hydrolysate from herring (Clupea harengus). J Food Sci. 1999;64:1000–04.10.1111/j.1365-2621.1999.tb12268.xSearch in Google Scholar
[22] Bouaouina H, Desrumaux A, Loisel C, Legrand J. Functional properties of whey proteins as affected by dynamic high-pressure treatment. Int Dairy J. 2006;16:275–84.10.1016/j.idairyj.2005.05.004Search in Google Scholar
[23] Suzuki M, Kobayashi Y, Hiraki Y, Nakata H, Shiomi K. Paramyosin of the disc abalone Haliotis discus discus: identification as a new allergen and cross-reactivity with tropomyosin. Food Chem. 2011;124:921–26.10.1016/j.foodchem.2010.07.020Search in Google Scholar
[24] Wang S, Zhang J, Jiao W, Li J, Xun X, Sun Y, et al. Scallop genome provides insights into evolution of bilaterian karyotype and development. Nat Ecol Evol. 2017;1:0120.10.1038/s41559-017-0120Search in Google Scholar
[25] Patwary MU. Isolation and characterization of a cDNA encoding an actin gene from sea scallop (Placopecten magellanicus). J Shellfish Res. 1996;15:265–70.Search in Google Scholar
[26] Ma H, Mai K, Liufu Z, Xu W. Cloning and characterization of an actin gene of Chlamys farreri and the phylogenetic analysis of mollusk actins. Chin J Oceanology Limnology. 2007;25:304–09.10.1007/s00343-007-0304-5Search in Google Scholar
[27] Bryant MJ, Flint HJ, Sin FYT. Isolation, characterization, and expression analysis of three actin genes in the New Zealand black-footed abalone, Haliotis iris. Marine Biotechnol. 2006;8:110–19.10.1007/s10126-005-5139-5Search in Google Scholar
[28] Bader S, Bez J, Eisner P. Can protein functionalities be enhanced by high-pressure homogenization? – A study on functional properties of lupin proteins. Procedia Food Sci. 2011;1:1359–66.10.1016/j.profoo.2011.09.201Search in Google Scholar
[29] Malhotra A, Coupland JN. The effect of surfactants on the solubility, zeta potential, and viscosity of soy protein isolates. Food Hydrocoll. 2004;18:101–08.10.1016/S0268-005X(03)00047-XSearch in Google Scholar
[30] Yu ZY, Jiang SW, Cao XM, Jiang ST, Pan LJ. Effect of high pressure homogenization (HPH) on the physical properties of taro (Colocasia esculenta (L) Schott). Pulp J Food Eng. 2016;177:1–8.10.1016/j.jfoodeng.2015.10.042Search in Google Scholar
[31] Shilpashree BG, Arora S, Chawla P, Vakkalagadda R, Sharma A. Succinylation of sodium caseinate and its effect on physicochemical and functional properties of protein. LWT Food Sci Technol. 2015;64:1270–77.10.1016/j.lwt.2015.07.008Search in Google Scholar
[32] Chen X, Xu X, Zhou G. Potential of high pressure homogenization to solubilize chicken breast myofibrillar proteins in water. Innov Food Sci Emerg Tech. 2016;33:170–79.10.1016/j.ifset.2015.11.012Search in Google Scholar
[33] Chen C, Chi Y, Xu W. Comparisons on the functional properties and antioxidant activity of spray-dried and freeze-dried egg white protein hydrolysate. Food and Bioprocess Technol. 2012;5:2342–52.10.1007/s11947-011-0606-7Search in Google Scholar
[34] Siddique MAB, Maresca P, Pataro G, Ferrari G. Effect of pulsed light treatment on structural and functional properties of whey protein isolate. Food Res Int. 2016;87:189–96.10.1016/j.foodres.2016.07.017Search in Google Scholar PubMed
[35] Hu H, Li C, Eunice CY, Wan L, Tian M, Pan S. The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocoll. 2013;32:303–11.10.1016/j.foodhyd.2013.01.016Search in Google Scholar
[36] Manoi KRSSH. Emulsification mechanisms and characterizations of cold, gel-like emulsions produced from texturized whey protein concentrate. Food Hydrocoll. 2009;23:1837–47.10.1016/j.foodhyd.2009.02.011Search in Google Scholar
[37] Shilpashree BG, Arora S, Chawla P, Tomar SK. Effect of succinylation on physicochemical and functional properties of milk protein concentrate. Food Res Int. 2015;72:223–30.10.1016/j.foodres.2015.04.008Search in Google Scholar
[38] Yuan B, Ren J, Zhao M, Luo D, Gu L. Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate. LWT Food Sci Technol. 2012;46:453–59.10.1016/j.lwt.2011.12.001Search in Google Scholar
© 2018 Walter de Gruyter GmbH, Berlin/Boston
