scholarly journals Condensation of glycosidic and aromatic structures on amino groups of β-lactoglobulin B via reductive alkylation. Solubility and emulsifying properties of the protein derivatives

1990 ◽  
Vol 70 (3) ◽  
pp. 205-215 ◽  
Author(s):  
C. Bertrand-Harb ◽  
B. Charrier ◽  
M. Dalgalarrondo ◽  
J. M. Chobert ◽  
T. Haertlé
Keyword(s):  
Emulsifying Properties ◽  
Reductive Alkylation ◽  
Amino Groups ◽  
Β Lactoglobulin

scholarly journals Physicochemical properties of three food proteins treated with transglutaminase

2004 ◽  
Vol 34 (4) ◽  
pp. 1219-1223 ◽  
Author(s):  
Luís Henrique de Barros Soares ◽  
Patrícia Melchionna Albuquerque ◽  
Francine Assmann ◽  
Marco Antônio Záchia Ayub
Keyword(s):  
Physicochemical Properties ◽  
Nitrogen Content ◽  
Soy Protein ◽  
Free Amino ◽  
Amino Nitrogen ◽  
Emulsifying Properties ◽  
Amino Groups ◽  
Emulsifying Activity ◽  
Food Proteins ◽  
Isolated Soy Protein

Three sources of food proteins were treated with microbial transglutaminase (EC 2.3.2.13) in order to assess changes in the physicochemical properties of reactivity, solubility, emulsification, and free amino groups of the formed polymers. Samples of lactic casein (LC), isolated soy protein (ISP), and hydrolysed animal protein (HAP), were incubated with the enzyme for one or two hours. LC and ISP showed a reduced solubility of 15% and 24% respectively, with HAP showing no alteration on solubility. Amino nitrogen content was 7%, 3% and 2% reduced for HAP, LC and ISP respectively. LC and ISP demonstrated lower emulsifying activity when they were enzymatically treated but the formed emulsions were stable, contrasting with HAP, which exhibited no changes in emulsifying properties.

Effect of high pressure homogenization on the structure and the interfacial and emulsifying properties of β-lactoglobulin

2018 ◽  
Vol 537 (1-2) ◽  
pp. 111-121 ◽  
Author(s):  
Ali Ali ◽  
Isabelle Le Potier ◽  
Nicolas Huang ◽  
Véronique Rosilio ◽  
Monique Cheron ◽  
...  
Keyword(s):  
High Pressure ◽  
High Pressure Homogenization ◽  
Emulsifying Properties ◽  
Β Lactoglobulin

Selective fluorescent labeling of amino groups of bovine pancreatic tryspin inhibitor by reductive alkylation

Biopolymers ◽  
1986 ◽  
Vol 25 (9) ◽  
pp. 1645-1658 ◽  
Author(s):  
Dan Amir ◽  
Daniel P. Levy ◽  
Yehuda Levin ◽  
Elisha Haas
Keyword(s):  
Fluorescent Labeling ◽  
Reductive Alkylation ◽  
Amino Groups

New Method for the Determination of Free Amino Groups in Intact Pure Proteins: Relationship to Available Lysine

1976 ◽  
Vol 59 (6) ◽  
pp. 1251-1254
Author(s):  
James M Purcell ◽  
Daniel J Quimby ◽  
James R Cavanaugh
Keyword(s):  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Free Amino ◽  
Amino Group ◽  
Amino Groups ◽  
Primary Amino ◽  
Available Lysine ◽  
Β Lactoglobulin ◽  
Group Concentration

Abstract A new rapid method for the quantitative and routine determination of free amino groups in intact pure proteins has been developed. Primary amino groups are labeled with fluorescamine and the labeled groups are detected by absorption spectroscopy in the range 375–390 nm. The amino group concentration can be determined in a few minutes without hydrolyzing the labeled protein and extracting a lysine derivative. The method was tested with the following proteins: lysozyme, α-lactalbumin, β-lactoglobulin, bovine serum albumin, ribonuclease, ribonuclease-S-peptide, and αsl-rasciii B. Application of this method to the estimation of available lysine is discussed.

Reversible reductive alkylation of amino groups in proteins

Biochemistry ◽  
1979 ◽  
Vol 18 (24) ◽  
pp. 5392-5399 ◽  
Author(s):  
Kieran F. Geoghegan ◽  
Donna M. Ybarra ◽  
Robert E. Feeney
Keyword(s):  
Reductive Alkylation ◽  
Amino Groups
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