Identification and Screening of Potential Bioactive Peptides with Sleep-Enhancing Effects in Bovine Milk Casein Hydrolysate

Author(s):  
Jingjing Qian ◽  
Lin Zheng ◽  
Guowan Su ◽  
Mingtao Huang ◽  
Donghui Luo ◽  
...  
2011 ◽  
Vol 63 (5) ◽  
pp. 398-404 ◽  
Author(s):  
David Sánchez ◽  
Modar Kassan ◽  
María del Mar Contreras ◽  
Rosalía Carrón ◽  
Isidra Recio ◽  
...  

1973 ◽  
Vol 20 (10) ◽  
pp. 473-477 ◽  
Author(s):  
I LIANG ◽  
ZENICHIRO HAMAUZU ◽  
SACHIO MATSUMOTO ◽  
DAIZO YONEZAWA

Peptides ◽  
2009 ◽  
Vol 30 (12) ◽  
pp. 2221-2227 ◽  
Author(s):  
Paul Guilloteau ◽  
Véronique Romé ◽  
Luc Delaby ◽  
François Mendy ◽  
Loic Roger ◽  
...  

1995 ◽  
Vol 62 (2) ◽  
pp. 339-348 ◽  
Author(s):  
Hajime Otani ◽  
Isao Hata

SUMMARYThe modulating effect of bovine milk casein components and their digests on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced or not induced by mitogens has been studied with a colorimetric assay using 3-(4, 5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. All the casein components and their digests tested had little mitogenic effect on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells. Intact κ-casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and Peyer's patch cells induced by mitogens such as lipopolysaccharide fromSalmonella typhimurium, concanavalin A, phytohaemagglutinin and pokeweed mitogen. In contrast, intact αsl-casein and β-casein had little effect. κ-Casein had an inhibitory effect after digesti on by pancreatin or trypsin, but not after pepsin or chymotrypsin digestion. Both pancreatin and trypsin digests of αsl-casein and -casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced by mitogens, whereas pepsin and chymotrypsin digests of both caseins were without effect. Moreover, the trypsin digest of each casein component had an inhibitory effect on mouse spleen lymphocyte proliferation in the absence of mitogen. Since trypsin is a major proteinase in pancreatin, the substrate specificity of trypsin seems to be important for the formation of the inhibitory peptides from casein components. These observations suggest that intact κ-casein and some peptides formed from milk casein components by the action of trypsin may suppress the immune responsiveness of neonates.


Biochemistry ◽  
1971 ◽  
Vol 10 (25) ◽  
pp. 4788-4793 ◽  
Author(s):  
S. H. C. Lin ◽  
R. K. Dewan ◽  
V. A. Bloomfield ◽  
C. V. Morr

2013 ◽  
Vol 80 (2) ◽  
pp. 227-232 ◽  
Author(s):  
Nissim Silanikove ◽  
Fira Shapiro ◽  
Uzi Merin ◽  
Gabriel Leitner

The aims of this study were to test the assumption that tissue-type plasminogen activator (t-PA) and plasminogen (PG) are closely associated with the casein micelle and form a functional complex that rules casein degradation. This assumption was essentially verified for bovine milk under conditions wherein the plasmin system was activated by treatment with casein hydrolysate. It was also shown that urokinase-type PA (u-PA), the second type of plasminogen activator present in milk, was not involved in casein degradation. In agreement with previous studies, we show that treatment with casein hydrolysate precipitously reduced mammary secretion, disrupted the tight junction integrity (increase in Na+ and decrease in K+ concentrations), induced hydrolysis of casein, and activated various elements of the innate and acquired immune system. In the present study, we have identified t-PA as the principal PA, which is responsible for the conversion of PG to plasmin. It was found that t-PA and plasminogen are present in freshly secreted milk (less than 10 min from its secretion), suggesting that they are secreted as a complex by the mammary gland epithelial cells. Further research is needed to provide the direct evidence to verify this concept.


1995 ◽  
Vol 62 (1) ◽  
pp. 115-122 ◽  
Author(s):  
Jeffrey H. White ◽  
Boris Zavizion ◽  
Kristen O'Hare ◽  
James Gilmore ◽  
Ming R. Guo ◽  
...  

SUMMARYThe type and relative amounts of plasminogen activator (PA) in different fractions of bovine milk obtained from 15 Holstein cows were examined. Raw milk was centrifuged to separate skim milk and a somatic cell pellet. PA was mainly localized within the casein fraction, being 42 times that in the serum, and in association with somatic cells. The predominant form of PA in milk casein was isolated from SDS-PAGE gel extracts and had a molecular mass of ∽75 kDa. Its activity was increased 41-fold (P < 0·01) in the presence of fibrin but was unaffected by the presence of amiloride, indicating that it was due to tissue-PA. The predominant forms of PA associated with milk somatic cells were isolated from SDS-PAGE gel extracts and had molecular masses of ∽ 30 and ∽ 50 kDa. The activity of both proteins was unaffected by the presence of fibrin but was dramatically reduced by the presence of amiloride, indicating that they represented urokinase-PA.


1959 ◽  
Vol 197 (1) ◽  
pp. 27-30 ◽  
Author(s):  
D. F. Magee ◽  
S. S. Hong

Evidence is presented that the chronic pancreatic fistula dogs can be used effectively to study pancreatic physiology on a daily output basis. By increasing the amount of a mixed diet fed or by adding fat to the diet the volume and protease and lipase activities can be increased. Additions of cellulose, milk, casein hydrolysate were ineffective. On the basal mixed diet neither volume, amylase nor protease increased independently of each other. Changes in one enzyme activity without the other or in volume without enzymes were seen with supplements of essential amino acids or soy flour. The possible mechanism of these effects is discussed.


1974 ◽  
Vol 342 (2) ◽  
pp. 313-321 ◽  
Author(s):  
R.K. Dewan ◽  
A. Chudgar ◽  
R. Mead ◽  
V.A. Bloomfield ◽  
C.V. Morr

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