NDLI: Nonruminant Nutrition Phytase , Other Enzymes , and Mineral Nutrition 1374 Characteristics of phytase secreted in saliva of the transgenic enviropig

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Nonruminant Nutrition Phytase , Other Enzymes , and Mineral Nutrition 1374 Characteristics of phytase secreted in saliva of the transgenic enviropig

Content Provider	Semantic Scholar
Author	Jakob, S. Maillard, Rainer Nore, Olivier Kwon, O. S. Wook, Jang Han, Yeon Kun Kim, Jeong Hyun Lee, Sang Hwi Min, Byoung Joon Lee, Woo Bung Miller, Hervine McLean Toplis, Paul Spears, W. Corns, M. D. Heugten, Eric Van Flowers, William L. Hill, Michael G. Sands, Jason S. Ragland, Denise Adeola, Olayiwola
Copyright Year	2002
Abstract	Thermolysin is a metalloendopeptidase that requires calcium to maintain its structural stability. The objective of this study was to evaluate the effect of calcium ions on the reaction products released during thermolysin hydrolysis of tryptic fragments from β-casein. Tryptic fragments β-CN 1-25 and β-CN 29-99 were isolated from a tryptic hydrolysate of purified β-casein. Both fragments were solubilized (2 mg.ml−1) in water or Tris buffer (50 mM) added with CaCl2 (0.1 and 10 mM), then hydrolysed at 40◦C with 0.01% of thermolysin. During hydrolysis, aliquots were taken over a 24 hours period and reaction products were identified by mass spectrometry (LC-MS and MS-MS). Results indicated that calcium ions enhanced the kinetics of reaction, and modified the peptidic profile resulting from thermolysin hydrolysis of both fragments. Specifically, the sequence β-CN 6-22 which contains 4 phosphoseryl residues was found in higher proportion in hydrolysate prepared without calcium than in its presence. Also, the presence of calcium seemed to promote the cleavage of the peptidic bound E11-I12, yielding to large amount of the sequence β-CN 6-11. Binding of calcium ions to phosphoseryl residues thus could influence the attack of β-casein by thermolysin and might be use to produce specific peptide sequences during hydrolysis of β-casein with thermolysin.
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://www.jtmtg.org/JAM/2002/abstracts/jnabs116.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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