KARAKTERISTIK KIMIA KONJUGAT ISOLAT PROTEIN KEDELAI-LAKTOSA YANG BERPOTENSI DALAM PENURUNAN ALERGENISITAS

Muhammad Hasriandy Asyhari, Nurheni Sri Palupi, Didah Nur Faridah

Abstract


Soy protein isolate (SPI) is a product from soybeans with great functionality thus is widely used as an ingredient in any formulation by food and beverage industries. Glycation is commonly done to improve protein functionality and reduce its allergenicity. This research aims to analyze the influence of incubation time of SPI and lactose on the degree of glycation of SPI-lactose conjugates, free amino acid and lactose bases, and to identify the molecular weight and intensity of the protein band of the SPI-lactose conjugate. SPIs were obtained by pH adjustment. The glycation of SPI and lactose was undertaken at pH 9.5, 95°C for 0, 30, 60 and 90 minutes. The determination of the glycation degree of the SPI-lactose conjugate was carried out using several methods, i.e. TBA-based method, HPLC and Bradford analysis. The profiles of the protein molecular weight was analyzed using SDS-PAGE. The results revealed that longer incubation time induced a greater degree of glycation. SDS-PAGE showed that the soybean sample had 13 protein bands with molecular weights ranging from 11.8 to 170.2 kDa. Glycation of SPI with lactose at 95°C could remove or lower the intensity of protein bands with molecular weight of 66.6; 56.1 and 30.9 kDa, which were presumed to be the major allergens in soybean.

Keywords


degree of glycation; glycation; lactose; soy protein isolate

Full Text:

PDF

References


Aissa AA, Aïder M. 2013. Lactose isomerization into lactulose in an electro-activation reactor and high-performance liquid chromatography (HP LC) monitoring of the process. J Food Eng 119: 115–124. DOI: 10.1016/j.jfoodeng.2013.05.011.

Amnuaycheewa P, de Mejia EG. 2010. Purification, characterisation, and quantification of the soy allergen profilin (Gly m 3) in soy products. Food Chem 119: 1671–1680. DOI: 10.1016/j.food chem.2009.09.034.

Astuti RM, Palupi NS, Zakaria FR. 2016. Allergic reactivity of bambara groundnut (Vigna sub-terranea) proteins. Food Agr Immunol 27: 535–546. DOI: 10.1080/09540105.2015.1129601.

Bielikowicz K, Wojtacha P, Kostyra E, Iwan M, Jarmołowska B, Kostyra H. 2010. Influence of glycation of wheat albumins and globulins on their immunoreactivity and physicochemical properties. J Food Nutr Sci 60: 335–340.

Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254. DOI: 10. 1016/0003-2697(76)90527-3.

Brady PN, Macnaughtan MA. 2015. Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights. Anal Biochem 491: 43–51. DOI: 10.10 16/j.ab.2015.08.027.

Bu G, Luo Y, Lu J, Zhang Y. 2010. Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reac-tion conditions. Food Agr Immunol 21: 143–156. DOI: 10.1080/09540100903452122.

Bu G, Zhang N, Chen F. 2015. The influence of gly-cosylation on the antigenicity, allergenicity, and structural properties of 11S-lactose conjugates. Food Res Int 76: 511–517. DOI: 10.1016/j.food res.2015.08.004.

Carpin M, Bertelsen H, Bech JK, Jeantet R, Risbo J, Schuck P. 2016. Caking of lactose: A critical re-view. Trends Food Sci Technol 53: 1–12. DOI: 10.1016/j.tifs.2016.04.002.

Drapala KP, Auty MAE, Mulvihill DM, O’Mahony JA. 2015. Improving thermal stability of hydrolysed whey protein-based infant formula emulsions by protein-carbohydrate conjugation. Food Res Int 88: 1–10. DOI: 10.1016/j. foodres.2016.01.028.

Hashemi SA, Ashtiani FZ. 2010. The isomerization kinetics of lactose to lactulose in the presence of sodium hydroxide at constant and variable pH. Food Bioprod Process 88: 181–187. DOI: 10.1016/j.fbp.2009.11.001.

Hidayat M, Kurnia D, Sujatno M, Sutadipura N, Setiawan. 2010. Perbandingan Kandungan makronutrisi dan isoflavon dari kedelai detam 1 dan wilis serta potensinya dalam menurun-kan berat badan. J Ilmu-ilmu Hayati dan Fis 12: 5–13.

Kusumasari S. 2017. Validasi Metode Deteksi Aler-gen Kedelai dan Aplikasinya dalam Pengem-bangan Isolat Protein Kedelai dan Susu Kedelai Hipoalergenik [Tesis]. Bogor: Fakultas teknologi Pertanian, Institut Pertanian Bogor.

Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteri-ophage T4. Nature 227: 680–685. DOI: 10.10 38/227680a0.

van de Lagemaat J, Manuel Silván J, Javier Moreno F, Olano A, Dolores del Castillo M. 2007. In vitro glycation and antigenicity of soy proteins. Food Res Int 40: 153–160. DOI: 10.1016/j.food res.2006.09.006.

Li W, Zhao H, He Z, Zeng M, Qin F, Chen J. 2016. Modification of soy protein hydrolysates by Maillard reaction: Effects of carbohydrate chain length on structural and interfacial properties. Colloid Surface B 138: 70–77. DOI: 10.1016/ j.colsurfb.2015.11.038.

Liu C, Wang H, Cui Z, He X, Wang X. 2007. Optimi-zation of extraction and isolation for 11S and 7S globulins of soybean seed storage protein. Food Chem 102: 1310–1316. DOI: 10.1016/j. foodchem.2006.07.017.

Liu G, Zhong Q. 2015. High temperature-short time glycation to improve heat stability of whey pro-tein and reduce color formation. Food Hydro-colloid 44: 453–460. DOI: 10.1016/j.foodhyd.20 14.10.006.

Ogawa T, Samoto M, Takahashi K. 2000. Soybean allergens and hypoallergenic soybean pro-ducts. J Nutr Sci Vitaminol 46: 271–279. DOI: 10.3177/jnsv.46.271.

de Oliveira FC, Coimbra JS dos R, de Oliveira EB, Zuñiga ADG, Rojas EEG. 2016. Food protein-polysaccharide conjugates obtained via the maillard reaction-a review. Crit Rev Food Sci 56: 1108–1125. DOI: 10.1080/10408398.2012. 755669.

Palupi NS, Sitorus SR, Kusnandar F. 2015. Pe-rubahan alergenisitas protein kacang kedelai dan kacang bogor akibat pengolahan dengan panas. J Teknol Industri Pangan 26: 222–231. DOI: 10.6066/jtip.2015.26.2.222.

Patel KN, Modi RB, Patel HG, Aparnathi KD. 2013. Browning, its chemistry and implications in dairy products: a review. Indo-Am J Agric Vet Sci 1: 1-12.

Seri A, Khorsand M, Rezaei Z, Hamedi A, Takhshid MA. 2017. Inhibitory effect of bunium persicum hydroalcoholic extract on glucose-induced albu-min glycation, oxidation, and aggregation in vitro. Iran J Med Sci 42: 369–376.

Shen Q, Yang R, Hua X, Ye F, Wang H, Zhao W, Wang K. 2012. Enzymatic synthesis and iden-tification of oligosaccharides obtained by trans-galactosylation of lactose in the presence of fructose using β-galactosidase from Kluy-vero-myces lactis. Food Chem 135: 1547–1554. DOI: 10.1016/j.foodchem.2012.05.115.

Speroni F, Milesi V, Añón MC. 2010. Interactions between isoflavones and soybean proteins : Applications in soybean-protein isolate pro-duction. LWT-Food Sci Technol 43: 1265–1270. DOI: 10.1016/j.lwt.2010.03.011.

Suseno R, Palupi NS, Prangdimurti E. 2016. Alerge-nisitas sistem glikasi isolat protein kedelai-fruktooligosakarida. Agritech 36: 450–458. DOI: 10.22146/agritech.16770

Verhoeckx KCM, Vissers YM, Baumert JL, Faludi R, Feys M, Flanagan S, Herouet-Guicheney C, Holzhauser T, Shimojo R, van der Bolt N, Wichers H, Kimber I. 2015. Food processing and allergenicity. Food Chem Toxicol 80: 223–240. DOI: 10.1016/j.fct.2015.03.005.

Wilson S, Blaschek K, Mejia EG De. 2005. Allerge-nic Proteins in Soybean: Processing and Re-duction of P34 Allergenicity. Nutr 63: 47–58. DOI: 10.1301/nr.2005.feb.47.

Wu H, Wang Q, Ma T, Ren J. 2009. Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Res Int 42: 343–348. DOI: 10. 1016/j.foodres.2008.12.006.

Xinmin W, Ruili Z, Zhihua L, Yuanhong W, Tingfu J. 2008. Determination of glucosamine and lactose in milk-based formulae by high-perfor-mance liquid chromatography. J Food Compos Anal 21: 255–258. DOI: 10.1016/j.jfca.2007.10. 006.




DOI: https://doi.org/10.6066/jtip.2018.29.1.39

Copyright (c) 2018 Jurnal Teknologi dan Industri Pangan

pISSN :   1979-7788

eISSN :   2087-751X


Visitor Statistic

 

 

Visitor Statistic

Visitor Statistic

Creative Commons License
This journal is published under the terms of the is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License