Rheological properties of soy protein hydrolysates obtained from limited enzymatic hydrolysis

LWT ◽  
2007 ◽  
Vol 40 (7) ◽  
pp. 1215-1223 ◽  
Author(s):  
B.P. Lamsal ◽  
S. Jung ◽  
L.A. Johnson
Keyword(s):  
Enzymatic Hydrolysis ◽  
Rheological Properties ◽  
Soy Protein ◽  
Protein Hydrolysates ◽  
Soy Protein Hydrolysates

Production of antioxidant soy protein hydrolysates by sequential ultrafiltration and nanofiltration

2013 ◽  
Vol 429 ◽  
pp. 81-87 ◽  
Author(s):  
Sahan Ranamukhaarachchi ◽  
Lena Meissner ◽  
Christine Moresoli
Keyword(s):  
Soy Protein ◽  
Protein Hydrolysates ◽  
Soy Protein Hydrolysates

Intracerebroventricular Administration of Soy Protein Hydrolysates Reduces Body Weight without Affecting Food Intake in Rats

2007 ◽  
Vol 63 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Nerissa Vaughn ◽  
Anthony Rizzo ◽  
Dolores Doane ◽  
J. Lee Beverly ◽  
Elvira Gonzalez de Mejia
Keyword(s):  
Body Weight ◽  
Food Intake ◽  
Soy Protein ◽  
Protein Hydrolysates ◽  
Intracerebroventricular Administration ◽  
Soy Protein Hydrolysates

scholarly journals Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates

2011 ◽  
Vol 20 (No. 1) ◽  
pp. 7-14 ◽  
Author(s):  
M. Hrčková ◽  
M. Rusňáková ◽  
J. Zemanovič
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Properties ◽  
Aqueous Dispersion ◽  
Protein Hydrolysates ◽  
Soy Flour ◽  
Degree Of Hydrolysis ◽  
Defatted Soy Flour ◽  
Sds Page ◽  
Soy Protein Hydrolysates ◽  
Hydrolysis Of

Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  

Calcium-binding ability of soy protein hydrolysates

2007 ◽  
Vol 18 (9) ◽  
pp. 1115-1118 ◽  
Author(s):  
Xiao Lan Bao ◽  
Mei Song ◽  
Jing Zhang ◽  
Yang Chen ◽  
Shun Tang Guo
Keyword(s):  
Soy Protein ◽  
Calcium Binding ◽  
Protein Hydrolysates ◽  
Binding Ability ◽  
Soy Protein Hydrolysates

scholarly journals The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis

Molekul ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. 145
Author(s):  
Sandra Hermanto ◽  
Aldi Octavio ◽  
Azrifitria Azrifitria ◽  
Susi Kusumaningrum
Keyword(s):  
Molecular Weight ◽  
Soy Protein ◽  
Reductase Inhibitor ◽  
Protein Hydrolysates ◽  
Molecular Weight Determination ◽  
Hmg Coa Reductase ◽  
Vitro Assay ◽  
Hmg Coa Reductase Inhibitor ◽  
Coa Reductase ◽  
Soy Protein Hydrolysates

The search for an HMG-CoA reductase inhibitor agent as a safe and inexpensive alternative treatment for hypercholesterolemia has been carried out using soy protein hydrolysates as one of the bioactive peptide sources. This study was conducted to explore the potency of soy protein hydrolysates as an anti hypercholesterolemia agent by an in vitro assay, through the inhibition capacity of the HMG-CoA (3-hydroxy-3-methyl glutaryl-coenzyme A) reductase enzyme as a key component of cholesterol biosynthesis. Sample preparation started with soy protein isolation through acid precipitation and separated by centrifugation. The samples were analyzed the proximate content and hydrolyzed by papain enzyme at concentration 0.2% (w/v), for 0-6 hours and at 37, 50, and 55 oC. The protein hydrolysates were subsequently evaluated for hydrolysis degree (% DH), hydrolysates profile with SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis), and anti-cholesterol assay through HMG-CoA reductase inhibition tests. The sample with the highest inhibition activity was fractionated using gel filtration chromatography (Sephadex G-10) and the molecular weight of fractions was characterized by LCMS QTOF (Liquid Chromatography-Mass Spectrometry Quadrupole Time-of-Flight) for molecular weight determination. The results indicated the optimum hydrolysis conditions of soy protein isolates were obtained at 3 hours incubation, at 50 °C with DH 33.39% and the inhibition value was 95.65% (protein concentration 39.21 μg / mL). LCMS data showed the molecular weight of fractionated peptides were 1514 and 2029 Da. We assumed that both peptides have the same affinity as previous peptides in inhibiting HMG-CoA reductase.

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