한국축산식품학회지 (Food Science of Animal Resources)

  • 제30권6호
  • /
  • Pages.923-929
  • /
  • 2010
  • /
  • 2636-0772(pISSN)
  • /
  • 2636-0780(eISSN)
한국축산식품학회 (Korean Society for Food Science of Animal Resources)
권호 표지
DOI QR코드

DOI QR Code

Production of Iron-Binding Peptides from Colostral Whey by Enzymatic Hydrolysis

  • Kim, Sang-Bum (Dairy Science Division, National Institute of Animal Science, Rural Development Administration) ;
  • Ku, Min-Jung (Dairy Science Division, National Institute of Animal Science, Rural Development Administration) ;
  • Cho, Won-Mo (Dairy Science Division, National Institute of Animal Science, Rural Development Administration) ;
  • Ki, Kwang-Seok (Dairy Science Division, National Institute of Animal Science, Rural Development Administration) ;
  • Kim, Hyeon-Shup (Dairy Science Division, National Institute of Animal Science, Rural Development Administration) ;
  • Nam, Myoung-Soo (Laboratory of Milk Food Biochemistry and Biotechnology, College of Agriculture and Life Sciences, Chungnam National University)
  • 투고 : 2010.08.25
  • 심사 : 2010.11.24
  • 발행 : 2010.12.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Colostral whey prepared from colostrum (pooled from first six post-partum milkings) was heated for 10 min at $100^{\circ}C$ Heated colostral whey was incubated with 1% enzymes (protein equivalent basis) for 15, 30, 60, 90, and 120 min at $50^{\circ}C$. Papain, pepsin, trypsin, and alcalase produced different degrees of hydrolysis (DH), 10.66%, 12.42%, 10.83%, and 25.31%, respectively, at an incubation time of 120 min. The SDS-PAGE reveals that significant amounts of bovine serum albumin (BSA), ${\beta}$-lactoglobulin (${\beta}$-LG), and ${\alpha}$-lactalbumin (${\alpha}$-LA) survived papain digestion. In contrast, pepsin completely removed BSA but not ${\beta}$-LG present in heated colostral whey. Alcalase completely eliminated BSA, ${\beta}$-LG, and ${\alpha}$-LA. This differential hydrolysis was confirmed by reversed-phase HPLC analysis. Using ion-exchange chromatography, fraction-1 (F-1) was obtained from alcalase hydrolysate at a NaCl gradient concentration of 0.25 M. Reversed-phase HPLC chromatograms of alcalase F-1 showed numerous small peaks, which probably indicate that a variety of new peptides were produced. Iron content of alcalase F-1 was 28.94 ppm, which was the highest among all enzyme fractions, whereas iron content of colostral whey was 36.56 ppm. Main amino acids contained in alcalase F-1 were Thr (15.45%), Glu (14.12%), and Ser (10.39%). Therefore, alcalase can be used to generate good iron-binding peptides in heated colostral whey, and the resulting iron-binding peptides could be suitable as a value-added food ingredient for food supplements.

키워드

참고문헌

  1. Adler-Nissen, J. (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 27, 1256-1262. https://doi.org/10.1021/jf60226a042
  2. Bradford, M. M. (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. https://doi.org/10.1016/0003-2697(76)90527-3
  3. Foley, J. A. and Otterby, D. E. (1978) Availability, storage, treatment, composition, and feeding value of surplus colostrum: A review. J. Dairy Sci. 61, 1033-1060. https://doi.org/10.3168/jds.S0022-0302(78)83686-8
  4. Fox, P. F. (1989) The milk protein system. In P. F. Fox (Ed.), Developments in dairy chemistry, London, UK: Elsevier Applied Science, Vol. 4, pp. 1-53.
  5. Georgiev, P. (2008) Differneces in chemical composition between cow colostrums and milk. Bulgarian J. V. Med. 11, 3- 12.
  6. Kim, S. B., Seo, I. S., Khan, M. A., Ki, K. S., Nam, M. S., and Kim, H. S. (2007) Separation of iron-binding protein whey through enzymatic hydrolysis. Int. Dairy J. 17, 625-631. https://doi.org/10.1016/j.idairyj.2006.09.001
  7. Larson, B. (1992) Immunoglobulins of the mammary secretions. In: Advanced dairy chemistry.p Fox. P. F. (ed). Elsevier Applied Science, London, UK, pp. 231-254.
  8. Liang, J., Han, B., Nout, M. J. R., and Hamer, R. J. (2009) Effect of soaking and phytase treatment on phytic acid, calcium, iron and zinc in rice fractions. Food Chem. 115, 789-794. https://doi.org/10.1016/j.foodchem.2008.12.051
  9. Liang, J., Han, B., Nout, M. J. R., and Hamer, R. J. (2008) Effect of soaking, germination and fermentation on phytic acid, total and in vitro soluble zinc in brown rice. Food Chem. 110, 821-828. https://doi.org/10.1016/j.foodchem.2008.02.064
  10. Moore, S., Spackman, D. H., and Stein, W. H. (1958) Automatic recording apparatus for use in the chromatography of amino acids. Fed. Am. Soc. Exp. Biol. 17, 1107-1115.
  11. Pintado, M. E., Pintado, A. E., and Malcata, F. X. (1999) Controlled whey protein hydrolysis using two alternative proteases. J. Food Eng. 42, 1-13. https://doi.org/10.1016/S0260-8774(99)00094-1
  12. Playford, R. J., Macdonald, C. E., and Johnson, W. S. (2000) Colostrum and milk-derived peptide growth factors for the treatment of gastrointestinal disorders. Am. J. Clin. Nutr. 72, 5-14.
  13. Rebeca, B. D., Pena-Vera, M. T., and Diaz-Castaneda, M. (1991) Production of fish protein hydrolysates with bacterial proteases: Yield and nutritional value. J. Food Sci. 56, 309-314. https://doi.org/10.1111/j.1365-2621.1991.tb05268.x
  14. Rose, D., Davies, D. T., and Yaguchi, M. (1969) Quantitative determination of the major components of casein mixture by column chromatography on DEAE-cellulose. J. Dairy Sci. 52, 8-11. https://doi.org/10.3168/jds.S0022-0302(69)86491-X
  15. SAS (2002) SAS User's Guide, Version 6.02. SAS Institute Inc., NC.
  16. Symth, M. and Fitz-Gerald, R. J. (1998) Relationship between some characteristics of WPC hydrolysates and the enzyme complement in commercially available proteinase preparations. Int. Dairy J. 8, 819-827. https://doi.org/10.1016/S0958-6946(98)00121-6
  17. Sukan, G. and Andrews, A. T. (1982) Application of the plastein reaction to caseins and to skim milk powder. I. Protein hydrolysis and plastein formation. J. Dairy Res. 49, 265-278. https://doi.org/10.1017/S0022029900022366
  18. WHO (2001) Iron deficiency anemia: Assessment, prevention and control. Geneva, Switzerland: World Health Organisation, pp. 1-22.

피인용 문헌

  1. Reduction in antigenesity of whey protein by alcalase vol.40, pp.4, 2013, https://doi.org/10.7744/cnujas.2013.40.4.359
  2. Strategies of producing bioactive peptides from milk proteins to functionalize fermented milk products vol.63, 2014, https://doi.org/10.1016/j.foodres.2014.06.002
  3. Impact of the environmental conditions and substrate pre-treatment on whey protein hydrolysis: A review vol.57, pp.2, 2017, https://doi.org/10.1080/10408398.2014.959115
  4. Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides vol.9, pp.10, 2010, https://doi.org/10.3390/foods9101406