Changes of protein profiles in pork and beef meat caused by high hydrostatic pressure treatment

Csehi, Barbara; Szerdahelyi, Emőke; Pásztor-Huszár, Klára; Salamon, B.; Tóth, Adrienn; Zeke, Ildikó; Jónás, Gábor; Friedrich, LÃ¡szlÃ3

doi:10.1556/066.2016.45.4.14

Cited by 5 publications

(3 citation statements)

References 19 publications

(20 reference statements)

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“…Appropriate diluted 10 µL of soybean milk and enzyme-hydrolyzed soybean milk samples were loaded into the wells. Gel was stained with 0.2% Coomassie Brilliant Blue (R250, Bio-Rad) for 30 min and a gel image was taken using a Gel Doc (Bio-Rad, USA) [44].…”

Section: Determination Of Molecular Weight Of Soybean Milk Proteins Amentioning

confidence: 99%

Antioxidant and Antibacterial Peptides from Soybean Milk through Enzymatic- and Membrane-Based Technologies

et al. 2019

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Enzymatic hydrolysis of soybean milk proteins with cysteine protease papain was performed in an advanced bioreactor, operated with batch mode. In soybean milk protein hydrolysis reaction, enzyme and substrate ratio and reaction temperature were varied, ranging from 0.029:100-0.457:100 and 30-60 • C, respectively. The degree of hydrolysis of soybean milk proteins was increased with increase of enzyme and substrate (soybean milk protein) ratio. However, the degree of hydrolysis was increased due to change of reaction temperature from 30 • C to 60 • C with enzyme and substrate ratio 0.229:100 and was reduced when hydrolysis reaction was performed with enzyme and substrate ratio 0.11:100 at hydrolysis temperature 60 • C. Antioxidant capacity of enzyme-treated milk had a similar trend with degree of hydrolysis. In a later exercise, a membrane bioreactor was adopted for continuous production of antioxidant and antibacterial peptides from soybean milk. The membrane bioreactor was operated for 12 h with constant feeding. Ceramic-made tubular membrane with a pore size 20 nm was used. Application of static turbulence promoter in a membrane separation process was investigated and its positive effects, with respect to higher permeate flux and lower energy consumption in filtration process, were proven. Antioxidant capacity and antibacterial activity against Bacillus cereus of enzyme-hydrolyzed milk and permeate from membrane were confirmed.

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Section: Determination Of Molecular Weight Of Soybean Milk Proteins Amentioning

confidence: 99%

Antioxidant and Antibacterial Peptides from Soybean Milk through Enzymatic- and Membrane-Based Technologies

et al. 2019

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“…De-staining of gel was performed with 50% (volume basis) methanol-water and 10% (volume basis) acetic acid at RT. An image of the gel was taken using a Gel Doc System 2000 (Bio-Rad, CA, USA) [ 71 ]. The image was imported into the freeware program ImageJ, version 1.5 (National Institutes of Health (NIH), Bethesda, MD, USA) for quantifying the band intensities of different proteins.…”

Section: Methodsmentioning

confidence: 99%

Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives

et al. 2022

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The objective of the investigation was to understand the biochemical activities of hydrolysate of soybean milk protein (SMP). Hydrolysis was carried out by different concentrations of papain (0.008 g·L−1, 0.016 g·L−1, 0.032 g·L−1 and 0.064 g·L−1). The antioxidant capacity was measured by the ferric-reducing ability of plasma (FRAP) and 2,2-Diphenyl-1-picrylhydrazyl (DPPH) assays. The anti-angiotensin activity of hydrolysate was measured by the recombinant angiotensin converting enzyme and substrate Abz-FRK(Dnp)-P. The contributions of the Kunitz trypsin inhibitor (KTI) and Bowman–Birk inhibitor (BBI) on antigenicity, and the in vitro digestion of papain-hydrolyzed SMP were studied. Rabbit polyclonal anti-KTI and anti-BBI antibodies together with peroxidase-labelled goat anti-Rb IgG secondary antibody were used to identify the antigenicity of KTI and BBI in unhydrolyzed and papain-hydrolyzed SMP. The antioxidant capacity and anti-angiotensin activity of SMP were increased after the papain hydrolysis of SMP. The KTI- and BBI-specific antigenicity were reduced in SMP by increasing the concentration of papain. However, there was interaction between papain-hydrolyzed SMP and trypsin in native gel, while interaction with chymotrypsin was absent. The interaction between trypsin and SMP was reduced due to the hydrolysis of papain in a concentration-dependent manner. According to the in vitro gastrointestinal digestion simulation protocol (Infogest), the digestibility of SMP was not statistically increased.

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“…After 30 min of gel staining, de-staining of gel was performed with 50% (volume basis) of methanol-water and 10% (volume basis) of acetic acid. Gel image was captured using a Gel Doc XR+ System (Bio-Rad, Hercules, USA) and the molecular weight of bands were determined using Quantity One software program (version 4.6) (Bio-Rad, Hercules, CA, USA) [74].…”

Section: Understanding Of Hydrolysis Of Liquid Milk Protein Concentratementioning

confidence: 99%

Production of Liquid Milk Protein Concentrate with Antioxidant Capacity, Angiotensin Converting Enzyme Inhibitory Activity, Antibacterial Activity, and Hypoallergenic Property by Membrane Filtration and Enzymatic Modification of Proteins

et al. 2020

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Liquid milk protein concentrate with different beneficial values was prepared by membrane filtration and enzymatic modification of proteins in a sequential way. In the first step, milk protein concentrate was produced from ultra-heat-treated skimmed milk by removing milk serum as permeate. A tubular ceramic-made membrane with filtration area 5 × 10−3 m2 and pore size 5 nm, placed in a cross-flow membrane house, was adopted. Superior operational strategy in filtration process was herein: trans-membrane pressure 3 bar, retention flow rate 100 L·h−1, and implementation of a static turbulence promoter within the tubular membrane. Milk with concentrated proteins from retentate side was treated with the different concentrations of trypsin, ranging from 0.008–0.064 g·L−1 in individual batch-mode operations at temperature 40 °C for 10 min. Subsequently, inactivation of trypsin in reaction was done at a temperature of 70 °C for 30 min of incubation. Antioxidant capacity in enzyme-treated liquid milk protein concentrate was measured with the Ferric reducing ability of plasma assay. The reduction of angiotensin converting enzyme activity by enzyme-treated liquid milk protein concentrate was measured with substrate (Abz-FRK(Dnp)-P) and recombinant angiotensin converting enzyme. The antibacterial activity of enzyme-treated liquid milk protein concentrate towards Bacillus cereus and Staphylococcus aureus was tested. Antioxidant capacity, anti-angiotensin converting enzyme activity, and antibacterial activity were increased with the increase of trypsin concentration in proteolytic reaction. Immune-reactive proteins in enzyme-treated liquid milk protein concentrate were identified with clinically proved milk positive pooled human serum and peroxidase-labelled anti-human Immunoglobulin E. The reduction of allergenicity in milk protein concentrate was enzyme dose-dependent.

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Changes of protein profiles in pork and beef meat caused by high hydrostatic pressure treatment

Cited by 5 publications

References 19 publications

Antioxidant and Antibacterial Peptides from Soybean Milk through Enzymatic- and Membrane-Based Technologies

Antioxidant and Antibacterial Peptides from Soybean Milk through Enzymatic- and Membrane-Based Technologies

Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives

Production of Liquid Milk Protein Concentrate with Antioxidant Capacity, Angiotensin Converting Enzyme Inhibitory Activity, Antibacterial Activity, and Hypoallergenic Property by Membrane Filtration and Enzymatic Modification of Proteins

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