Isolation and Identification of Peptides from the Diafiltration Permeate of the Water-Soluble Fraction of Cheddar Cheese

1998 ◽  
Vol 46 (11) ◽  
pp. 4512-4517 ◽  
Author(s):  
Manuela Fernández ◽  
Tanoj K. Singh ◽  
Patrick F. Fox
1997 ◽  
Vol 64 (3) ◽  
pp. 433-443 ◽  
Author(s):  
TANOJ K. SINGH ◽  
PATRICK F. FOX ◽  
ÁINE HEALY

Several peptides were isolated from the diafiltration retentate, prepared using 10 kDa membranes, of the water-soluble extract from a commercial mature Cheddar cheese and identified by amino acid sequencing and mass spectrometry. Most of the peptides were from the N-terminal half of β-casein, but peptides from αs1- and αs2-caseins were also identified; the extract also contained α-lactalbumin. Identified peptides showed the important role played by lactococcal cell envelope proteinases in the degradation of primary proteolytic products from αs1- and β- caseins, produced by chymosin and plasmin respectively. Plasmin seemed to be involved in the hydrolysis of αs2-casein. Several phosphopeptides were identified and the action of phosphatase on these peptides was evident.


1991 ◽  
Vol 58 (3) ◽  
pp. 363-372 ◽  
Author(s):  
Dolores Gonzalez de Llano ◽  
M. Carmen Polo ◽  
Mercedes Ramos

SummaryThe blue cheese nitrogenous fractions soluble in water and in 5% phosphotungstic acid (PTA) were analysed by HPLC after 3–180 d ripening. In the water-soluble fraction, in addition to four or five major peaks corresponding to amino acids, there were many minor peaks, which increased during ripening. The low molecular mass peptides, soluble in 5% PTA, showed ripening-induced increments. A method combining precipitation with 5% PTA, gel permeation and subsequent HPLC was used to isolate some peptides of cheese. Four peptides containing between seven and ten residues were isolated and their amino acid composition and N-terminal residues determined.


2014 ◽  
Vol 91 (5) ◽  
pp. 473-481 ◽  
Author(s):  
Guiai Jiao ◽  
Xiangjin Wei ◽  
Gaoneng Shao ◽  
Lihong Xie ◽  
Zhonghua Sheng ◽  
...  

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.


Chemosphere ◽  
2010 ◽  
Vol 78 (11) ◽  
pp. 1301-1312 ◽  
Author(s):  
S.M. Rodrigues ◽  
B. Henriques ◽  
J. Coimbra ◽  
E. Ferreira da Silva ◽  
M.E. Pereira ◽  
...  

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