Isolation and Purification of Thiamine Binding Protein from Mung Bean

Gunarti, Dwirini Retno; Rahmi, Hanifah; Sadikin, Mohamad

doi:10.4308/hjb.20.1.1

Cited by 9 publications

(7 citation statements)

References 13 publications

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“…Prolamin, however, has not yet been isolated and characterised from mung bean. Aside from these major proteins, components comprising the other 15% of mung bean protein components have not yet been extensively studied to date, except for trypsin inhibitor ( 24 ), non-specific lipid transfer proteins (nsLTP) ( 25 ) and thiamine-binding proteins ( 26 ) ( Table 2 ).…”

Section: Mung Bean Seed Proteinsmentioning

confidence: 99%

Mung bean proteins and peptides: nutritional, functional and bioactive properties

Zhu¹,

Sun²,

Fitzgerald³

2018

Food & Nutrition Research

178

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To date, no extensive literature review exists regarding potential uses of mung bean proteins and peptides. As mung bean has long been widely used as a food source, early studies evaluated mung bean nutritional value against the Food and Agriculture Organization of the United Nations (FAO)/the World Health Organization (WHO) amino acids dietary recommendations. The comparison demonstrated mung bean to be a good protein source, except for deficiencies in sulphur-containing amino acids, methionine and cysteine. Methionine and cysteine residues have been introduced into the 8S globulin through protein engineering technology. Subsequently, purified mung bean proteins and peptides have facilitated the study of their structural and functional properties. Two main types of extraction methods have been reported for isolation of proteins and peptides from mung bean flours, permitting sequencing of major proteins present in mung bean, including albumins and globulins (notably 8S globulin). However, the sequence for albumin deposited in the UniProt database differs from other sequences reported in the literature. Meanwhile, a limited number of reports have revealed other useful bioactivities for proteins and hydrolysed peptides, including angiotensin-converting enzyme inhibitory activity, anti-fungal activity and trypsin inhibitory activity. Consequently, several mung bean hydrolysed peptides have served as effective food additives to prevent proteolysis during storage. Ultimately, further research will reveal other nutritional, functional and bioactive properties of mung bean for uses in diverse applications.

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Section: Mung Bean Seed Proteinsmentioning

confidence: 99%

Mung bean proteins and peptides: nutritional, functional and bioactive properties

Zhu¹,

Sun²,

Fitzgerald³

2018

Food & Nutrition Research

178

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“…Mung bean, also known as green gram, is a small, green-colored legume widely cultivated throughout Asia [1]. It is a popular legume in countries such as Indonesia and China where its consumption is associated with positive health outcomes [2,3]. Mung bean flour is commonly made into a paste and incorporated into bread and desserts [4].…”

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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“…The reaction of a heavy metal salt with a protein usually leads to an insoluble metal protein salt. [17][18][19][20][21][22][23][24][25][26][27]…”

Section: Discussionmentioning

confidence: 99%

Properties of A Thiamine Binding Protein Purified from Mung Bean

Gunarti¹,

Kartika

Sadikin³

2020

Self Cite

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Materials Mung Bean Thiamine Binding Protein (MBTBP) used was the result of post-affinity chromatography with levels of 1446 μg/mL that had been identified and analyzed. KH 2 PO 4 , Na 2 HPO 4 , NaCl, NaOH, BSA, sodium EDTA, iodoacetate, hydrogen peroxide, β-mercaptoethanol, HgCl 2 , AgNO 3 , thiamine, buffer sulphate, dialysis tubing cellulose membrane was purchased from Sigma-Aldrich. Methods Protein assay Concentration of protein was determined by the method of Warburg-Christian using bovine serum albumin as the standard. 5 Effect of temperature and storage time on MBTBP stability MBTBP powder was known to be concentrated and diluted to a concentration of 250 μg/mL in aliquoting and stored at-20°C, 4°C and 37°C with storage time of 3 days, 7 days, 14 days and 30 days. 6,7 Furthermore, protein levels were measured using a standard BSA curve.

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Isolation and Purification of Thiamine Binding Protein from Mung Bean

Cited by 9 publications

References 13 publications

Mung bean proteins and peptides: nutritional, functional and bioactive properties

Mung bean proteins and peptides: nutritional, functional and bioactive properties

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

Properties of A Thiamine Binding Protein Purified from Mung Bean

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