Electro-membrane filtration for the selective isolation of bioactive peptides from an ?s2-casein hydrolysate

2002 ◽  
Vol 80 (6) ◽  
pp. 599-609 ◽  
Author(s):  
Gerrald Bargeman ◽  
Joukje Houwing ◽  
Isidra Recio ◽  
Geert-Henk Koops ◽  
Caroline van der Horst
2020 ◽  
Vol 31 (2) ◽  
pp. 188-196
Author(s):  
Diana Lestari ◽  
◽  
Joshua Evan ◽  
Maggy Thenawidjaja Suhartono ◽  
◽  
...  

Milk bioactive peptides are derivative of milk protein produced either through enzymatic activity, digestive processes, or fermentation, that give functional properties. The study aimed to obtain bioactive peptides fraction derived from goat’s milk casein through hydrolysis by papain, analyze the profiles of protein and peptides, and also test the antioxidative activity. The casein isolate was hydrolyzed by papain in a ratio of 100: 0.5 (v/v) at pH 7.0 and 50ºC. Analysis of protein concentration was carried out by the Bradford method and protein profile by SDS-PAGE. Antioxidant assay was carried out by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) method. A 1,000 ppm ascorbic acid solution was used as positive control. Peptide fractionation was done by membrane filtration with a cut off of 10 kD and 30 kDa. The protein concentration of casein hydrolysates decreased significantly after hydrolysis process with papain. The electrophoresis results showed six protein bands in casein with molecular weight of 7-33 kDa. After the hydrolysis process, all hydrolysates only contained two protein bands with molecular weights of 8 and 5 kDa. The hydrolysis process increased the antioxidant activity of the casein. P0 and P2 hydrolysates had the highest antioxidant activity, and fractions with the highest antioxidant activity were fraction <10 kDa from P0 hydrolysate at 67.89% and 10-30 kDa from P2 hydrolysate at 73.82%. Molecular weight and hydrolysis time affected the antioxidant activity of the hydrolysates. Peptides below 30 kDa have antioxidant activity, whereas those above 30 kDa do not have any antioxidant activity. The antioxidant activity of the peptides decreases upon hydrolysis for more then 2 minutes.


1993 ◽  
Vol 39 (1) ◽  
pp. 46-51 ◽  
Author(s):  
D. I. Kurtböke ◽  
N. E. Murphy ◽  
K. Sivasithamparam

A method was developed to reduce the numbers of thermophilic bacteria on isolation plates, which in turn facilitated the detection and isolation of thermophilic actinomycetes. The method involves exposing the test material to bacteriophage suspensions prior to inoculation on isolation plates. This method was applied to composted eucalyptus bark samples, which were then inoculated on R8 and 1/2 TSA + 0.2% casein hydrolysate agar plates. The phage susceptibility of thermophilic bacteria provided a selective means of reducing their numbers on isolation plates and hence increased the numbers of Thermomonospora, Saccharopolyspora rectivirgula, and thermophilic Streptomyces spp. on these media in comparison with the numbers recorded from control plates.Key words: bacteriophage, thermophilic bacteria, thermophilic actinomycetes, composted eucalyptus bark.


2013 ◽  
Vol 52 (1) ◽  
pp. 231-239 ◽  
Author(s):  
Imran Irshad ◽  
Ara Kanekanian ◽  
Adrian Peters ◽  
Tariq Masud

Desalination ◽  
2002 ◽  
Vol 149 (1-3) ◽  
pp. 369-374 ◽  
Author(s):  
G. Bargeman ◽  
G.-H. Koops ◽  
J. Houwing ◽  
I. Breebaart ◽  
H.C. van der Horst ◽  
...  

2000 ◽  
Vol 80 (1) ◽  
pp. 175-185 ◽  
Author(s):  
Gerrald Bargeman ◽  
Monique Dohmen-Speelmans ◽  
Isidra Recio ◽  
Martin Timmer ◽  
Caroline van der Horst

Foods ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2573
Author(s):  
Erica Pontonio ◽  
Marco Montemurro ◽  
Gina Valeria De Gennaro ◽  
Valerio Miceli ◽  
Carlo Giuseppe Rizzello

Aiming at valorizing the ricotta cheese exhausted whey (RCEW), one of the most abundant by-products from the dairy industry, a biotechnological protocol to obtain bioactive peptides with angiotensin-I-converting enzyme (ACE)--inhibitory activity was set up. The approach was based on the combination of membrane filtration and fermentation. A Lactobacillus helveticus strain selected to be used as starter for the fermentation of the ultrafiltration protein-rich retentate (R-UF) obtained from RCEW. The fermented R-UF was characterized by a high anti-ACE activity. Peptides responsible for the bioactivity were purified and identified through nano-LC–ESI–MS/MS. The sequences identified in the purified active fractions of the fermented R-UF showed partial or complete overlapping with previously reported κ-casein antihypertensive fragments. The fermented R-UF was spray-dried and used to enrich ricotta cheese at different fortification level (1 and 5% w/w). An integrated approach including the assessment of the microbiological, chemical, functional, textural, and sensory properties was used to characterize the fortified products. A significantly higher anti-ACE activity was found in the ricotta cheese fortified with fermented R-UF as compared to the control and to the samples obtained with the unfermented R-UF fraction at the same levels of fortification. In particular, a 100 g portion of the ricotta cheese produced at 5% fortification level contained circa 30 mg of bioactive peptides. The fortification led to a moderate acidification, increased hardness and chewiness, and decreased the milk odor and taste of the ricotta cheese as compared to the control, while flavor persistence and sapidity improved.


2019 ◽  
Vol 16 (6) ◽  
pp. 371-375
Author(s):  
Jung-Whan Chon ◽  
Dong-Hyeon Kim ◽  
Dongryeoul Bae ◽  
Kwang-Young Song ◽  
Hyunsook Kim ◽  
...  

2018 ◽  
Vol 84 (11) ◽  
pp. 23-27
Author(s):  
M. I. Degtev ◽  
A. A. Yuminova ◽  
A. S. Maksimov ◽  
A. P. Medvedev

The possibility of using an aqueous stratified system of antipyrine — sulfosalicylic acid — water for the selective isolation of scandium macro- and microquantities for subsequent determination is studied. The proposed extraction system eliminates the usage of toxic organic solvents. The organic phase with a volume of 1.2 to 2.0 ml, resulting from delamination of the aqueous phase containing antipyrine and sulfosalicylic acid is analysed to assess the possibility of using such systems for metal ions extraction. Condition necessary for the formation of such a phase were specified: the ratio of the initial components, their concentration, presence of inorganic salting out agents. The optimum ratio of antipyrine to sulfosalicylic acid is 2:1 at concentrations of 0.6 and 0.3 mol/liter in a volume of the aqueous phase of 10 ml. The obtained phase which consists of antipyrinium sulfosalicylate, free antipyrine and water, quantitatively extracts macro- and microquantities of scandium at pH = 1.54. Macro- and microquantities of yttrium, terbium, lanthanum, ytterbium and gadolinium are not extracted under the aforementioned conditions thus providing selective isolation of scandium from the bases containing yttrium, ytterbium, terbium, lanthanum, and gadolinium.


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