Isolation of low-molecular albumins of 2S fraction from soybean (Glycine max (L.) Merrill).

Galbas, Mariola; Porzucek, Filip; Woźniak, Anna; Słomski, Ryszard; Selwet, Marek

doi:10.18388/abp.2013_1958

Cited by 6 publications

(6 citation statements)

References 10 publications

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“…Previous studies have shown that different types of media have been successfully applied for the isolation of different enzymes. Among these media, the most commonly applied solvents were water, buffers or surfactants (Diaz et al, 2007, Abbasi et al, 2011, Galbas et al, 2013. In the present study two extractants, water and McIlvaine buffer at pH 5.0, were examined (90 ml against 15 g of orange peels).…”

Section: Isolation Of Pgmentioning

confidence: 99%

Enhanced production of polygalacturonase in solid-state fermentation: selection of the process conditions, isolation and partial characterization of the enzyme

Zasłona

Trusek-Hołownia

2015

Acta Biochim Pol

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Polygalacturonase (PG) production by Penicillium chrysogenum during solid-state fermentation was accompanied by decomposition of orange peels. A leaching procedure was developed through the selection of solvent, time and intensity of stirring. A maximum PG activity was observed after 48 h peel inoculation. Further cultivation decreased the enzyme activity significantly, up to 60% of the maximum PG activity. During fermentation, a rapid acidification of the solid medium which inhibited the pectinolytic enzyme, was observed. Buffering agents with different pH values and different ionic strengths were examined to identify the most suitable medium to avoid this problem. Buffer addition counteracted acidification and enhanced active protein production, which was observed for all of the applied pH values (6.5-8.0) of the buffering agent. The most satisfactory results were obtained when using the highest pH at 8.0. The protein content and PG activity increased from 3.5 mg/g and 1.09 U/g to 7.7 mg/g and 7.11 U/g during cultivation, with uncontrolled and pH-controlled medium, respectively. Measurements at wide pH and temperature ranges indicated an optimum for PG activity at pH 5.0 and 43°C; however, high thermal stability corresponded to lower temperatures, and a temperature of 37°C is thus recommended. Under these conditions, the operational stability was determined to be t1/2=570 h.

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Section: Isolation Of Pgmentioning

confidence: 99%

Enhanced production of polygalacturonase in solid-state fermentation: selection of the process conditions, isolation and partial characterization of the enzyme

Zasłona

Trusek-Hołownia

2015

Acta Biochim Pol

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“…In plants, albumins can be proteins stored in seeds to be used during germination and growth [15]. The isolation and characterization of some albumins in multiple legumes, such as lentils, soybeans and winged beans, has already been performed [16][17][18]. There are currently two main entries for mung bean albumin in the UniProt Database; Q9FRT8 is a reviewed entry detailing a 10 kDa protein fragment.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Potential of Mung Bean (Vigna radiata) Albumin Peptides Produced by Enzymatic Hydrolysis Analyzed by Biochemical and In Silico Methods

Kusumah

Hernandez

Mejı́a

2020

Foods

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The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity (ORAC) assay. Peeled raw mung bean was ground into flour and mixed with buffer (pH 8.3, 1:20 w/v ratio) before being stirred, then filtered using 3 kDa and 30 kDa molecular weight cut-off (MWCO) centrifugal filters to obtain albumin fraction. The albumin fraction then underwent enzymatic hydrolysis using either gastrointestinal enzymes (pepsin and pancreatin) or thermolysin. Peptides in the hydrolysates were sequenced. The peptides showed low ABTS radical-scavenging activity (90–100 μg ascorbic acid equivalent/mL) but high ferrous ion chelating activity (1400–1500 μg EDTA equivalent/mL) and ORAC values (>120 μM Trolox equivalent). The ferrous ion chelating activity was enzyme- and hydrolysis time-dependent. For thermolysin hydrolysis, there was a drastic increase in ferrous ion chelating activity from t = 0 (886.9 μg EDTA equivalent/mL) to t = 5 min (1559.1 μg EDTA equivalent/mL) before plateauing. For pepsin–pancreatin hydrolysis, there was a drastic decrease from t = 0 (878.3 μg EDTA equivalent/mL) to t = 15 (138.0 μg EDTA equivalent/mL) after pepsin was added, but this increased from t = 0 (131.1 μg EDTA equivalent/mL) to t = 15 (1439.2 μg EDTA equivalent/mL) after pancreatin was added. There was no significant change in ABTS radical scavenging activity or ORAC values throughout different hydrolysis times for either the thermolysin or pepsin–pancreatin hydrolysis. Overall, mung bean hydrolysates produced peptides with high potential antioxidant capacity, being particularly effective ferrous ion chelators. Other antioxidant assays that use cellular lines should be performed to measure antioxidant capacity before animal and human studies.

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“…This subunit is an allergen of soybean (Ebisawa et al, 2013) for humans, but it is also reported that the subunit as 2S albumin has anticancer activity against HeLa cells (Galbas, Porzucek, Woźniak, Słomski, & Selwet, 2013;Hirai, 2004;Losso, 2008;Lule, Garg, Pophaly, & Tomar, 2015;Pabona et al, 2013;Park, Jeong, & Lumen, 2007;Singh, Vij, & Hati, 2014). The subunit in soybean protein has many healthy functions and effects.…”

Section: Resultsmentioning

confidence: 99%

Lipopolysaccharide neutralizing protein inMiso, Japanese fermented soybean paste

Sasaki

Ngoc

Nishikawa

et al. 2020

Journal of Food Science

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Miso, a fermented paste made from soybeans, is used traditionally for seasoning of food. It has been a protein and nitrogen source since ancient times in Japan because of its high nutritional value. Furthermore, it has important health functions such as the estrogen‐like activity of isoflavones, anti‐oxidation, and angiotensin‐converting‐enzyme inhibition activity. Moreover, it has activity for neutralization of lipopolysaccharide (LPS) from Escherichia coli. Nevertheless, the mechanisms of that activity remain unclear. For this study, we purified and identified the proteins responsible for LPS‐neutralization. After proteins were isolated from a miso extract using Blue native polyacrylamide gel electrophoresis, a protein found at 10 to 30 kDa on the polyacrylamide gel was identified using nano LC‐MS/MS as 2S albumin in soybean (Glycine max). The protein had two LPS binding motifs: SKWQHQ (22 amino acid residues) and EKQKKKMEKE (131 amino acid residues). The protein in miso was found to have LPS neutralization activity, as assayed by prostaglandin D2 (PGD2) production from macrophage cells. The PGD2 production by macrophage cells was inhibited by LPS‐neutralizing protein (LNP) from miso. Particularly, 50 mg/mL of LNP solution and LPS (10 µg/mL) inhibited production of PGD2 from the cells. The data were inferred as significantly different (P < 0.05) from statistical analyses by analysis of variance testing and Tukey tests. The 2S albumin in soybean is LNP, an LPS‐neutralizing protein, produced in miso. Practical Application A protein from miso fermented soy paste neutralizes an Escherichia coli intestinal bacterial product, lipopolysaccharide (LPS), which causes intestinal inflammation. Miso and its protein are anticipated for use as a probiotic agent to prevent intestinal inflammation in humans and domestic animals. Miso is useful not only as a seasoning for food, but also as a health‐functional food because it is an LPS‐neutralizing agent.

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Isolation of low-molecular albumins of 2S fraction from soybean (Glycine max (L.) Merrill).

Cited by 6 publications

References 10 publications

Enhanced production of polygalacturonase in solid-state fermentation: selection of the process conditions, isolation and partial characterization of the enzyme

Enhanced production of polygalacturonase in solid-state fermentation: selection of the process conditions, isolation and partial characterization of the enzyme

Antioxidant Potential of Mung Bean (Vigna radiata) Albumin Peptides Produced by Enzymatic Hydrolysis Analyzed by Biochemical and In Silico Methods

Lipopolysaccharide neutralizing protein inMiso, Japanese fermented soybean paste

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