Research Article
BibTex RIS Cite

COMPARISON OF DIFFERENT METHODS FOR BETA LACTOGLOBULIN ISOLATION

Year 2018, Volume: 4 Issue: 1, 1 - 8, 01.01.2018

Ezgi Demir Özer , Zübeyde Öner

https://doi.org/10.3153/JFHS18001

Abstract

The aim of this
study was to introduce a simple, high efficient and less expensive method for
isolation of β-Lg from whey. Anion exchange chromatography, pepsin enzyme
treatment and ultrafiltration tecniques were preferred for isolation process to
compare differences. In addition to, centrifuge ultrafiltration techniques were
using for the first time for isolation of β-Lg from whey.  Physicochemical analysis of whey samples
indicated that protein and β-Lg content in whey samples changed from 0.07 to 0.8% and 0.24 to 0.29 g/L, respectively. Treatment with the use of
pepsin enzyme, anion exchanges chromatography and ultrafiltration techniques,
resulted to β-Lg of 1.43, 6.56 and 43.59 folds respectively. Our results showed
that ultrafiltration techniques are rapid and efficient that allows high
protein yield and has advantages over other methods since it preserves the
native structure of β-Lg. Additionally, when the
enzymatic hydrolysis was used together with ultrafiltration technique, it was
found efficient and pure than the enzymatic hydrolysis together with dialyse membrane.
Also this study concluded that pepsin enzyme treatment and anion exchange
chromatography are economic methods but they are not efficient enough and very
time consuming. However isolation efficiency can be
increased the use of isolation methods together.

Keywords

Beta lactoglobulin Whey Ultrafiltration Anion exchange chromatography Pepsin enzyme

References

  • Aich, R., Batabyal, S. & Joardar, S.N. (2015). Isolation and purification of beta-lactoglobulin from cow milk. Veterinary World, 8, 621-624.
  • Bhattacharjee, S., Bhattacharjee, C. & Datta, S. (2006). Studies on the fractionation of β-lactoglobulin from casein whey using ultrafiltration and ion-exchange membrane chromatography. Journal of Membrane Science, 275(1), 141-150.
  • Bottomley, R. (1991). Process for obtaining concentrates having a high α-lactalbumin content from whey. US Patent, Patent number: 5,008, 376.
  • Chatterton, D.E., Smithers, G., Roupas, P. & Brodkorb, A. (2006). Bioactivity of β-lactoglobulin and α-lactalbumin—Technological implications for processing. International Dairy Journal, 16(11), 1229-1240.
  • Cheang, B., & Zydney, A. L. (2003). Separation of α‐lactalbumin and β‐lactoglobulin using membrane ultrafiltration. Biotechnology and Bioengineering, 83(2), 201-209.
  • Cheang, B., & Zydney, A. L. (2004). A two-stage ultrafiltration process for fractionation of whey protein isolate. Journal of Membrane Science, 231(1), 159-167.
  • De Wit, J. (1998). Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science, 81(3), 597-608.
  • Elgar, D.F., Norris, C.S., Ayers, J.S., Pritchard, M., Otter, D.E., & Palmano, K.P. (2000). Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene–divinylbenzene. Journal of Chromatography A, 878(2), 183-196.
  • Fox, P. (2003). Milk proteins: general and historical aspects Advanced Dairy Chemistry—1 Proteins (pp. 1-48): Springer. ISBN 978-1-4419-8602-3
  • Guo, M., Fox, P., Flynn, A., & Kindstedt, P. (1995). Susceptibility of β-Lactoglobulin and Sodium Caseinate to Proteolysis by Pepsin and Trypsin. Journal of Dairy Science, 78(11), 2336-2344.
  • Hernández-Ledesma, B., Recio, I., & Amigo, L. (2008). β-Lactoglobulin as source of bioactive peptides. Amino Acids, 35(2), 257-265.
  • Jang, H.D., & Swaisgood, H.E. (1990). Disulfide bond formation between thermally denatured β-lactoglobulin and κ-casein in casein micelles. Journal of Dairy Science, 73(4), 900-904.
  • Karagözlü, C., & Bayarer, M. (2004). Peyniraltı suyu proteinlerinin fonksiyonel özellikleri ve sağlık üzerine etkileri. Ege Üniv. Ziraat Fakültesi Dergisi, 41, 197-207.
  • Kinekawa, Y.-I., & Kitabatake, N. (1996). Purification of β-Lactoglobulin from Whey Protein Concentrate by Pepsin Treatment. Journal of Dairy Science, 79(3), 350-356.
  • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685.
  • Lieske, B., Konrad, G., & Faber, W. (1997). A new spectrophotometric assay for native β-lactoglobulin in raw and processed bovine milk. International Dairy Journal, 7(12), 805-812.
  • Lozano, J.M., Giraldo, G.I., & Romero, C. M. (2008). An improved method for isolation of β-lactoglobulin. International Dairy Journal, 18(1), 55-63.
  • Morr, C., & Ha, E. (1993). Whey protein concentrates and isolates: processing and functional properties. Critical Reviews in Food Science & Nutrition, 33(6), 431-476.
  • Muller, A., Chaufer, B., Merin, U., & Daufin, G. (2003). Purification of alpha-lactalbumin from a prepurified acid whey: Ultrafiltration or precipitation. Le Lait, 83(6), 439-451.
  • Outinen, M. (2010). Effect of pre-treatment of cheese milk on the composition and characteristics of whey and whey products. TKK Dissertation 212, Aalto University, p. 44. ISBN 978-9-5260- 3006-7
  • Reddy, I.M., Kella, N.K., & Kinsella, J.E. (1988). Structural and conformational basis of the resistance of beta-lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry, 36(4), 737-741.
  • Sannier, F., Bordenave, S., & Piot, J. (2000). Purification of goat β-lactoglobulin from whey by an ultrafiltration membrane enzymic reactor. Journal of Dairy Research, 67(01), 43-51.
  • Şanlidere Aloğlu, H. (2013). The effect of various heat treatments on the antioxidant capacity of milk before and after simulated gastrointestinal digestion. International Journal of Dairy Technology, 66(2), 170-174.
  • Stojadinovic, M.,Burazer, L., Ercili-Cura,D., Sancho, A.,Buchert, J.,Velickovica T.C. & Stanic-Vucinica, D. (2012). One-step method for isolation and purification of native β-lactoglobulin. Journal of the Science of Food and Agriculture, 92, 1432-1440
  • Tunçtürk, Y., Andiç, S., & Ocak, E. (2010). Homojenizasyon ve pastörizasyonun Beyaz Peynir ve Peyniraltı Suyu Bileşimine Etkisi. Gıda/The Journal of Food, 35(5), 339-345.
  • Ye, X., Yoshida, S., & Ng, T. (2000). Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography. The International Journal of Biochemistry & Cell Biology, 32(11), 1143-1150.
  • Yerlikaya, O., Kınık, Ö., & Akbulut, N. (2010). Peyniraltı Suyunun Fonksiyonel Özellikleri ve Peyniraltı Suyu Kullanılarak Üretilen Yeni Nesil Süt Ürünleri. Gıda/The Journal of Food, 35(4), 289-296.
  • Young, V. R. (1994). Adult amino acid requirements: the case for a major revision in current recommendations. The Journal of Nutrition, 124(8 Suppl), 1517S-1523S.

Year 2018, Volume: 4 Issue: 1, 1 - 8, 01.01.2018

Ezgi Demir Özer , Zübeyde Öner

https://doi.org/10.3153/JFHS18001

Abstract

References

  • Aich, R., Batabyal, S. & Joardar, S.N. (2015). Isolation and purification of beta-lactoglobulin from cow milk. Veterinary World, 8, 621-624.
  • Bhattacharjee, S., Bhattacharjee, C. & Datta, S. (2006). Studies on the fractionation of β-lactoglobulin from casein whey using ultrafiltration and ion-exchange membrane chromatography. Journal of Membrane Science, 275(1), 141-150.
  • Bottomley, R. (1991). Process for obtaining concentrates having a high α-lactalbumin content from whey. US Patent, Patent number: 5,008, 376.
  • Chatterton, D.E., Smithers, G., Roupas, P. & Brodkorb, A. (2006). Bioactivity of β-lactoglobulin and α-lactalbumin—Technological implications for processing. International Dairy Journal, 16(11), 1229-1240.
  • Cheang, B., & Zydney, A. L. (2003). Separation of α‐lactalbumin and β‐lactoglobulin using membrane ultrafiltration. Biotechnology and Bioengineering, 83(2), 201-209.
  • Cheang, B., & Zydney, A. L. (2004). A two-stage ultrafiltration process for fractionation of whey protein isolate. Journal of Membrane Science, 231(1), 159-167.
  • De Wit, J. (1998). Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science, 81(3), 597-608.
  • Elgar, D.F., Norris, C.S., Ayers, J.S., Pritchard, M., Otter, D.E., & Palmano, K.P. (2000). Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene–divinylbenzene. Journal of Chromatography A, 878(2), 183-196.
  • Fox, P. (2003). Milk proteins: general and historical aspects Advanced Dairy Chemistry—1 Proteins (pp. 1-48): Springer. ISBN 978-1-4419-8602-3
  • Guo, M., Fox, P., Flynn, A., & Kindstedt, P. (1995). Susceptibility of β-Lactoglobulin and Sodium Caseinate to Proteolysis by Pepsin and Trypsin. Journal of Dairy Science, 78(11), 2336-2344.
  • Hernández-Ledesma, B., Recio, I., & Amigo, L. (2008). β-Lactoglobulin as source of bioactive peptides. Amino Acids, 35(2), 257-265.
  • Jang, H.D., & Swaisgood, H.E. (1990). Disulfide bond formation between thermally denatured β-lactoglobulin and κ-casein in casein micelles. Journal of Dairy Science, 73(4), 900-904.
  • Karagözlü, C., & Bayarer, M. (2004). Peyniraltı suyu proteinlerinin fonksiyonel özellikleri ve sağlık üzerine etkileri. Ege Üniv. Ziraat Fakültesi Dergisi, 41, 197-207.
  • Kinekawa, Y.-I., & Kitabatake, N. (1996). Purification of β-Lactoglobulin from Whey Protein Concentrate by Pepsin Treatment. Journal of Dairy Science, 79(3), 350-356.
  • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685.
  • Lieske, B., Konrad, G., & Faber, W. (1997). A new spectrophotometric assay for native β-lactoglobulin in raw and processed bovine milk. International Dairy Journal, 7(12), 805-812.
  • Lozano, J.M., Giraldo, G.I., & Romero, C. M. (2008). An improved method for isolation of β-lactoglobulin. International Dairy Journal, 18(1), 55-63.
  • Morr, C., & Ha, E. (1993). Whey protein concentrates and isolates: processing and functional properties. Critical Reviews in Food Science & Nutrition, 33(6), 431-476.
  • Muller, A., Chaufer, B., Merin, U., & Daufin, G. (2003). Purification of alpha-lactalbumin from a prepurified acid whey: Ultrafiltration or precipitation. Le Lait, 83(6), 439-451.
  • Outinen, M. (2010). Effect of pre-treatment of cheese milk on the composition and characteristics of whey and whey products. TKK Dissertation 212, Aalto University, p. 44. ISBN 978-9-5260- 3006-7
  • Reddy, I.M., Kella, N.K., & Kinsella, J.E. (1988). Structural and conformational basis of the resistance of beta-lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry, 36(4), 737-741.
  • Sannier, F., Bordenave, S., & Piot, J. (2000). Purification of goat β-lactoglobulin from whey by an ultrafiltration membrane enzymic reactor. Journal of Dairy Research, 67(01), 43-51.
  • Şanlidere Aloğlu, H. (2013). The effect of various heat treatments on the antioxidant capacity of milk before and after simulated gastrointestinal digestion. International Journal of Dairy Technology, 66(2), 170-174.
  • Stojadinovic, M.,Burazer, L., Ercili-Cura,D., Sancho, A.,Buchert, J.,Velickovica T.C. & Stanic-Vucinica, D. (2012). One-step method for isolation and purification of native β-lactoglobulin. Journal of the Science of Food and Agriculture, 92, 1432-1440
  • Tunçtürk, Y., Andiç, S., & Ocak, E. (2010). Homojenizasyon ve pastörizasyonun Beyaz Peynir ve Peyniraltı Suyu Bileşimine Etkisi. Gıda/The Journal of Food, 35(5), 339-345.
  • Ye, X., Yoshida, S., & Ng, T. (2000). Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography. The International Journal of Biochemistry & Cell Biology, 32(11), 1143-1150.
  • Yerlikaya, O., Kınık, Ö., & Akbulut, N. (2010). Peyniraltı Suyunun Fonksiyonel Özellikleri ve Peyniraltı Suyu Kullanılarak Üretilen Yeni Nesil Süt Ürünleri. Gıda/The Journal of Food, 35(4), 289-296.
  • Young, V. R. (1994). Adult amino acid requirements: the case for a major revision in current recommendations. The Journal of Nutrition, 124(8 Suppl), 1517S-1523S.
There are 28 citations in total.

Details

Subjects Food Engineering
Journal Section Articles
Authors

Ezgi Demir Özer 0000-0002-3525-5172

Zübeyde Öner 0000-0003-2557-0731

Publication Date January 1, 2018
Submission Date February 9, 2017
Published in Issue Year 2018Volume: 4 Issue: 1

Cite

APA Demir Özer, E., & Öner, Z. (2018). COMPARISON OF DIFFERENT METHODS FOR BETA LACTOGLOBULIN ISOLATION. Food and Health, 4(1), 1-8. https://doi.org/10.3153/JFHS18001
 Download Cover Image

16339

Journal is licensed under a

CreativeCommons Attribtion-ShareAlike 4.0 International Licence  14627 1331027042
Diamond Open Access refers to a scholarly publication model in which journals and platforms do not charge fees to either authors or readers.

Open Access Statement:

This is an open access journal which means that all content is freely available without charge to the user or his/her institution. Users are allowed to read, download, copy, distribute, print, search, or link to the full texts of the articles, or use them for any other lawful purpose, without asking prior permission from the publisher or the author. This is in accordance with the BOAI definition of open access.

Archiving Policy:

27222

Archiving is done according to ULAKBİM "DergiPark" publication policy (LOCKSS).