DIFFERENT APPROACHES IN ANALYZING CHYMOSIN PURITY

##plugins.themes.bootstrap3.article.sidebar##

PDF (English)
Објавено: Dec 1, 2019

##plugins.themes.bootstrap3.article.main##

T. Nestorovski
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia
L. Velkoska – Markovska
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia
S. Srbinovska
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia
E. Miskoska – Milevska
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia
B. Petanovska – Ilievska
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia
Z.T. Popovski
Ss. Cyril and Methodius University in Skopje, Faculty of Agricultural Sciences and Food - Skopje, Republic of North Macedonia

Апстракт

Chymosin is a specific proteolytic enzyme found in rennet, and is the key enzyme in cheese production classified in the aspartic endopeptidases (EC 3.4.23.4). The aim of this study was to determine the purity of different commercially available chymosins and its equivalents using electrophoretic and chromatographic techniques. Chymosins produced by the company Chr. Hansen, CHY-MAX 200 and CHY-MAX Plus, CHY-MAX PowderExtra NB, as well as Maxiren 1800 Granulate from the company DSM, Sirnik from SZR – Travnik, Kraljevo and Planika from Mikroprocessing, Bileca were used as materials for this study. The purity level of the commercially available enzymes was analyzed using electrophoretic (sodium dodecyl sulfate polyacrylamide gel electrophoresis or SDS-PAGE) and chromatographic (Rapid Resolution Liquid Chromatography or RRLC) techniques. Results showed no presence of undeclared protein fractions due to inappropriate purification process in the samples except for CHY-MAX М 200 which had two protein fractions, most likely as a result of a polymorphism. All the CHY-MAX and Maxiren samples have chymosin as the active component (36 kDa), except for Planika and Sirnik which have a natural protease from R. miehei. Chromatographic analysis showed that beside the active component (chymosin), the preservative sodium benzoate was present in varying concentrations in all but CHY-MAX PowderExtra NB.

Downloads

Download data is not yet available.

##plugins.themes.bootstrap3.article.details##

Издание
Том 73 Бр. 3 (2019): Journal of Agricultural, Food and Environmental Sciences, JAFES
Рубрика
Articles

Референци

Agboola, S., Chen, S. and Zhao, J. (2004). Formation of bitter peptides during ripening of ovine milk cheese made with different coagulants (in English, French). Lait (EDP Sciences), 84 (6): 567–578. doi:10.1051/lait:2004032. Retrieved 2007-12-31
Attallah, A. G. (2007). Characters of Chymosin Gene Isolated from Different Animal Sources at Molecular Level. Journal of Applied Sciences Research, 3 (9): 904-907
El-Sohaimy Elsayed, S. A., Hafez, E. and El Saadani, M. A. (2010). Cloning and In Vitro-Transcription of Chymosin Gene in E. coli. The Open Nutraceuticals Journal, 3: 63-68.
Fox, P. F., McSweeney, P., Cogan, M. T., Guinee, P. T. (2004). Cheese: Major cheese groups. Academic Press: 2.
Gastaldi, E., Trial, N., Guillaume, C., Bourret, E., Gontard, N. and Cuq, J. L. (2003). Effect of Controlled κ-Casein Hydrolysis on Rheological Properties of Acid Milk Gels. J Dairy Sci., 86 (3): 704-11.
PFIZER CENTRAL RESEARCH (1988). International submission on chymosin. Submitted to WHO by Pfizer, Inc., Groton, CT, USA. Szecsi, P. B. (1992). The aspartic proteases. Scandinavian Journal of Clinical and Laboratory Investigation, 52: 5-22.
Tamime, A. (1993). Modern Dairy Technology, edited by R. K. Robinson, Vol. 1, pp. 49–220. London: Elsevier Applied Science.
Wésolowski-Louvel, M., Breunig K. D., and Fukuhara H. Kluyveromyceslactis. In: K. Wolf, editor. Non-conventional yeast in biotechnology. Heidelberg: Springer- Verlag, 1996: p. 139-201.
Wick Macdonald (2010). Laboratory Manual- SDS PAGE reagents and SDS-PAGE Gel Formulae.