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Production of Iron-Binding Peptides from Colostral Whey by Enzymatic Hydrolysis
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 Title & Authors
Production of Iron-Binding Peptides from Colostral Whey by Enzymatic Hydrolysis
Kim, Sang-Bum; Ku, Min-Jung; Cho, Won-Mo; Ki, Kwang-Seok; Kim, Hyeon-Shup; Nam, Myoung-Soo;
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Colostral whey prepared from colostrum (pooled from first six post-partum milkings) was heated for 10 min at Heated colostral whey was incubated with 1% enzymes (protein equivalent basis) for 15, 30, 60, 90, and 120 min at . 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), -lactoglobulin (-LG), and -lactalbumin (-LA) survived papain digestion. In contrast, pepsin completely removed BSA but not -LG present in heated colostral whey. Alcalase completely eliminated BSA, -LG, and -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.
Colostral whey;hydrolysis;alcalase;iron-binding peptide;
 Cited by
Alcalase에 의한 유청단백질 가수분해물의 항원성 저감 효과,유재민;렌친핸드;;정석근;백승희;남명수;

농업과학연구, 2013. vol.40. 4, pp.359-365 crossref(new window)
Reduction in antigenesity of whey protein by alcalase, Korean Journal of Agricultural Science, 2013, 40, 4, 359  crossref(new windwow)
Strategies of producing bioactive peptides from milk proteins to functionalize fermented milk products, Food Research International, 2014, 63, 71  crossref(new windwow)
Impact of the environmental conditions and substrate pre-treatment on whey protein hydrolysis: A review, Critical Reviews in Food Science and Nutrition, 2017, 57, 2, 418  crossref(new windwow)
Adler-Nissen, J. (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 27, 1256-1262. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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.

Georgiev, P. (2008) Differneces in chemical composition between cow colostrums and milk. Bulgarian J. V. Med. 11, 3- 12.

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. crossref(new window)

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.

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. crossref(new window)

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. crossref(new window)

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.

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. crossref(new window)

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.

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. crossref(new window)

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. crossref(new window)

SAS (2002) SAS User's Guide, Version 6.02. SAS Institute Inc., NC.

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. crossref(new window)

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. crossref(new window)

WHO (2001) Iron deficiency anemia: Assessment, prevention and control. Geneva, Switzerland: World Health Organisation, pp. 1-22.