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At least 19 recordsLinked to original sources
PubMed1981

Molecular properties of the enzymic phytohemagglutinin of mung bean.

Mung bean seeds possess a tetrameric galactose-binding protein that displays two types of activities: (a) a hemagglutinin activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric form, which possesses both enzymic and hemagglutinin activities, to a monomeric form which possesses enzymic activity only. This observation suggests that the enzymic phytohemagglutinin is an aggregated form of a monomeric alpha-galactosidase. The tetrameric alpha-galactosidase has a pH optimum of about pH 7.0, while the monomeric form displays a pH optimum of 5.6. Circular dichroism difference spectra and inhibition studies suggest that aggregation induces conformational changes in the subunits sufficient to alter their enzymatic properties. The possibility of in vivo changes in subunit equilibria, when combined with the accompanying alterations in activity, provides a new concept worthy of consideration with respect to the physiological role of phytohemagglutinins.

Calcium-Binding Proteins↗
PubMed1999

Effect of Wild-Type and Mutant Plant Growth-Promoting Rhizobacteria on the Rooting of Mung Bean Cuttings.

Mung bean cuttings were dipped in solutions of wild type and mutant forms of the plant growth-promoting rhizobacterium Pseudomonas putida GR12-2 and then incubated for several days until roots formed. The bacteria P. putida GR12-2 and P. putida GR12-2/aux1 mutant do not produce detectable levels of the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase, whereas P. putida GR12-2/acd36 is an ACC deaminase minus mutant. All bacteria produce the phytohormone indole-3-acetic acid (IAA), and P. putida GR12-2/aux1 overproduces it. Treatment of cuttings with the above-mentioned bacteria affected the rates of ethylene production in the cuttings in a way that can be explained by the combined effects of the activity of ACC deaminase localized in the bacteria and bacterial produced IAA. P. putida GR12-2 and P. putida GR12-2/acd36-treated cuttings had a significantly higher number of roots compared with cuttings rooted in water. In addition, the wild type influenced the development of longer roots. P. putida GR12-2/aux1 stimulated the highest rates of ethylene production but did not influence the number of roots. These results are consistent with the notion that ethylene is involved in the initiation and elongation of adventitious roots in mung bean cuttings.

Journal Article↗
PubMed1983

Proteinases involved in the degradation of trypsin inhibitor in germinating mung beans.

The mung bean (Vigna radiata (L.) Wilczek) trypsin inhibitor (MBTI) is rapidly modified by limited proteolysis during the early stages of seedling growth. Using an electrophoretic assay that separates the unmodified inhibitor (MBTI-F) and the first two modified species (MBTI-E and -C), a pH optimum of approximately 4 was found for the modification reaction. The inhibitor modifying activity is initially low in ungerminated seeds, with the reaction F leads to E being the primary reaction catalyzed. Activity catalyzing the production of MBTI-C appears on the first day of germination. This activity (F leads to E leads to C) increases up to 6 days after inhibition, at which time the cotyledons begin to abscise. The activity converting MBTI-F and -E to MBTI-C was strongly inhibited by phenylmethylsulfonyl fluoride (3.3 mM) but only weakly by iodoacetate (9 mM) and not at all by pepstatin A (9 microM), leupeptin (18 microM), or EDTA (5 mM). These results suggest the involvement of proteinases other than the major endopeptidase of the germinating seed, vicilin peptidohydrolase. This conclusion is further supported by gel filtration of the extracts of cotyledons on Sephacryl S-200. At least three proteinases are present in germinated cotyledons capable of modifying MBTI-F to MBTI-C and/or -E. All are distinguishable from vicilin peptidohydrolase on the basis of their molecular weight and inhibition by low molecular weight organic reagents.

Chromatography, Gel↗
PubMed1977

The effect of calcium on the respiratory responses of mung bean mitochondria.

Purified mung bean hypocotyl mitochondria were examined for their capacity to carry out respiration-dependent accumulation of calcium. The addition of 0.1-1.0 mM calcium to mung bean mitochondria supplemented with succinate gave no stimulation of state 4 respiration even in the presence of inorganic phosphate and the ionophoretic antibiotic A-23187. Even at high calcium concentrations, no transient changes in the respiratory activity occurred and subsequent addition of ADP initiated a further state 3 response. Although the additions of calcium resulted in a rapid H+ ejection, it was insensitive to lanthanum and uncoupling agents. Similarly, additions of calcium failed to initiate any transient changes in the oxidation-reduction states of either pyridine nucleotides or cytochrome b. Direct spectrophotometric recordings of absorbance changes of murexide revealed no respiration-linked calcium transport. It is proposed that although mung bean mitochondria possess a respiration-linked electrochemical potential gradient it would appear that this potential cannot be expressed as calcium transport even at high ion concentrations, probably due to a low calcium membrane permeability.

Anaerobiosis↗
PubMed1996

Purification, characterisation and steady state kinetic properties of cytosolic pyruvate kinase free of phosphoenol pyruvate phosphatase activity from germinating mung beans (Vigna radiata L.)

Mung bean pyruvate kinase (PK) practically free from PEP-phosphatase has been purified about 36 fold. The enzyme is irreversibly inactivated on desalting by gel filtration or dialysis (without EDTA). The inactivation is also observed in the presence of ATP, Mg2+ or thiols but is prevented by a non-proteinous, heat stable, small molecular mass factor present in the mung bean extract. Mung bean PK has a molecular mass of 210 kDa. It shows single exponential decay of activity at various temperatures (-4 to 60 degrees C). The Km of PEP and ADP are found to be 0.12 and 0.24 mM, respectively at pH 6.5, when the enzyme is saturated with the second substrate. The Km values for PEP and ADP are 0.05 and 0.16 mM, at pH 8.5 and 0.09 and 0.17 mM, respectively at pH 7.5. The optimum pH is 7.5. The enzyme shows an absolute requirement for Mg2+ (Km 0.43 mM) or Mn2+ ions (Km 0.125 mM). Potassium ions are not essential but activate the enzyme in the presence of Mg2+ or Mn2+ ions. ATP shows competitive inhibition with ADP and non-competitive with PEP. Kinetic studies at different pHs and effects of ATP suggest the formation of a ternary complex (E.ADP.PEP) by a combination of random and compulsory ordered pathways depending on the experimental conditions.

Acid Phosphatase↗
PubMed1989

A growth analysis of waterlogging damage in mung bean (Phaseolus aureus).

Mung beans (Phaseolus aureus Roxb.) were grown for 2 weeks in gravel-vermiculite soilless mix in a growth chamber and subjected to a 1-week waterlogging period followed by a 1-week recovery period. Sequential harvests were made to determine the time course of effects of waterlogging and subsequent recovery on growth parameters by techniques of growth analysis. Root dry matter was the first to be affected, along with an increase in leaf dry matter and specific leaf weight. After a 1-week waterlogging period, specific leaf weight had more than doubled in the stressed plants. Leaf area declined in relation to the control plants as did the ratio of root dry matter to shoot dry matter. During the recovery period there was an increase in the dry matter allocation to the roots relative to the shoot. Specific leaf weight fell to control levels although the rate of leaf area elaboration did not increase during this time, suggesting a redistribution of stored assimilates from the leaves. Net assimilation rate increased during the waterlogging period, probably due to a restriction in root metabolism and reduced translocation out of the leaf rather than to an increase in photosynthesis. Net assimilation rate of waterlogged plants was severely reduced compared with control plants during the recovery period. Both relative growth rate and leaf area duration declined during the waterlogging period and declined further subsequent to the waterlogging treatment. The results illustrate the interrelationships between root and shoot carbon budgets in mung bean during response to the stress of waterlogging.

Environment, Controlled↗
PubMed1997

Mycoflora and mycotoxins in adzuki and mung beans produced in Ontario, Canada.

This is the first report on the detection of fumonisin B1 (FB1) in Fusarium-infected adzuki bean (Phaseolus angularis) and mung bean (Phaseolus aureus). The infected beans had either a mouldy appearance or a distinct discoloration. Seed coats of infected adzuki beans changed from dark red to light red and those of mung beans from green to dark or brownish green. Fusarium spp. isolated from mouldy and discoloured beans included F. avenaceum, F. culmorum, F. equiseti, F. graminearum, F. moniliforme, F. oxysporum, F. solani, F. sporotrichoides and a few unidentified species. Healthy beans without any apparent discoloration and diseased beans with discoloration and mouldy appearance were analysed for mycotoxins. Diacetoxyscripenol, deoxynivalenol and T-2 toxin (T-2) were not detected in either healthy or discoloured adzuki and mung bean samples by thin layer chromatography (TLC). FB1 was detected by TLC in discoloured adzuki and mung bean samples but not in the healthy samples. TLC results were confirmed by high performance liquid chromatography (HPLC). The quantification of FB1 by HPLC revealed that discoloured adzuki and mung bean samples contained 261 +/- 43.8, and 230 +/- 21.6 micrograms g-1 of FB1, respectively. This investigation emphasizes the need for more detailed research in dealing with possible mycotoxin contamination in various foodstuffs including legumes.

Canada↗
PubMed1982

Complete amino acid sequence of mung bean trypsin inhibitor.

The mung bean trypsin inhibitor has been found to be microheterogeneous at N-terminal region due to the presence of several isomers. After treatment with aminopeptidase M it becomes homogeneous and is suitable for sequence determination. Based on the determination of the structures of two active fragments the complete amino acid sequence of mung bean trypsin inhibitor has been elucidated. It consists of 72 amino acid residues with 7 pairs of disulfide bonds. The results show that this inhibitor belongs to the Bowman-Birk inhibitor family.

Amino Acid Sequence↗
PubMed2026

Bacillus subtilis isolated from medicinal plants rhizosphere effectively controls Cercospora leaf spot and improves plant growth in mung bean (Vigna radiata).

BACKGROUND: Mung bean is an important leguminous crop, which is reported to face devastating yield losses of up to 70% due to Cercospora leaf spot (CLS) disease. Traditional methods, such as the application of agrochemicals and fungicides, have been used to control CLS, but their intensive use has toxic effects on edible crops. METHODS: To find out a sustainable alternative, this study characterizes a strain, Bacillus subtilis Medicinal_04, isolated from Cannabis sativa rhizosphere and explores its role as an eco-friendly biofungicide and biostimulant. The species level identification of the isolate was confirmed by Average Nucleotide Identity (ANIb) and a digital DNA-DNA hybridization (dDDH). The antagonistic efficacy of B. subtilis Medicinal_04 against Cercospora canescens was evaluated in vitro as well as in planta assays. RESULTS: ANIb of 97.80% and a dDDH score of 85.90% against the reference B. subtilis str. 168. confirmed this isolate as B. subtilis. The in-vitro results showed that B. subtilis robustly inhibited C. canescens growth by 81.5%, strongly correlated with positive chitinolytic activity and a diverse genomic array of secondary metabolite biosynthetic gene clusters. The in planta results demonstrated that B. subtilis seed priming reduced disease incidence by 80 and 71.4%, while foliar application resulted in reductions of 90 and 85.7% for NM-51 and NM-20-21 varieties, respectively. Furthermore, fungicide application successfully reduced disease, however it caused noticeable phytotoxic reductions in root-shoot architecture and chlorophyll content. In contrast, biological interventions completely bypassed these trade-offs as B. subtilis application displayed improved root-shoot length, pod number, and chlorophyll content, while simultaneously enhancing antioxidative enzyme activities (SOD, POD, and CAT) and PR-1 gene expression. CONCLUSION: These findings demonstrate that B. subtilis Medicinal_04 has the potential to serve as a multifunctional biocontrol agent and is capable of securing high-level disease suppression and optimizing plant productivity, offering a valuable toolkit for climate-smart, sustainable agriculture.

Bacillus subtilis↗
PubMed1987

[The influence of germination on the nutritional value of wheat, mung beans and chickpeas].

The changes in nutrients during the germination of wheat, mung beans and chickpeas were investigated. Germination was performed under conditions commonly used in the household. The amount of water taken up during 4 days of germination varied from 159 g/100 g (chickpeas) to 450 g/100 g (mung beans). For all three seeds losses of dry matter and carbohydrates were observed. In wheat and mung beans, phytic acid was partially hydrolyzed. In mung beans, the total fat content decreased. Increases in the content of polyunsaturated fatty acids in wheat and of dietary fibre in wheat and mung beans were noted. At a constant level of crude protein, a measurable rise in limiting amino acids was observed in wheat and mung beans. Frequent watering during germination caused losses of Fe, between 9% and 21%, K (27% in chickpeas) and Cu (17% in chickpeas). Except for vitamin B6 in both legumes and vitamin B1 in chickpeas, accumulation of the vitamins under investigation (B1, B2, B6, C, E) was noted. Owing to these changes during germination, the nutritional value of the three seeds has been improved to various extents, most distinctly in wheat and least noticeably in chickpeas. Compared with other vegetables, sprouted seeds can be considered a valuable addition to the diet.

Fabaceae↗
PubMed1997

Regulatory properties and active site groups of cytosolic mung bean pyruvate kinase.

Properties of mung bean pyruvate kinase were studied and the active site groups were derived. Metabolites like AMP, glucose, glucose-6-phosphate, fructose-6-phosphate, fructose-1, 6-bisphosphate, 3-phospho-glycerate, isocitrate, malate and alpha-ketoglutarate had practically no effect on pyruvate kinase activity. Alanine, serine, glutamine, methionine and GMP had a weak activating effect on the enzyme. Some metabolites such as ATP, GTP, and UMP were found to be weakly inhibitory. Moderate to strong inhibition was observed with citrate, succinate, glutamate and oxalate. Inhibition brought about by ATP and citrate when present together showed synergistic effect. Inhibition by citrate was non-competitive with respect to both PEP and ADP suggesting the presence of a regulatory site. Mung bean pyruvate kinase showed half optimal activity at pH 6.6 and 8.9 at saturating concentrations of PEP, ADP and Mg2+. Small concentrations of the SH specific reagents, namely iodoacetamide (0.1 and 0.2 mM), N-ethylmaleimide(0.05-0.1 mM) and p-chloromercuribenzoate (0.1 mM) inactivated the enzyme; single exponential loss of activity was observed in each case. Photooxidation of the enzyme in the presence of methylene blue (100 and 200 micrograms/ml) and rose bengal (5 and 10 micrograms/ml) also led to a single exponential activity decay. When the enzyme was treated with diethyl pyrocarbonate (DEP), a time dependent exponential decay in its activity was observed with a parallel increase in absorbance at 240 nm. PEP protected the enzyme against inactivation by DEP. Reagents specific for tyrosine (iodine and tetranitromethane) and tryptophan residues (N-bromosuccinimide) residues had no effect. These observations confirm that SH and imidazole groups are vital for the activity of the enzyme.

Binding Sites↗
PubMed1989

Raw mung beans as a protein source for bred gilts.

A study involving 546 crossbred gilts from six seasons was conducted to evaluate raw mung beans as a partial replacement for soybean meal in diets for gilts during gestation. Gilts were randomly allotted to either a control sorghum grain-soybean meal diet or a diet in which a portion of the soybean meal was replaced with mung beans. In the first three seasons, gilts were fed diets in which the protein supplement was totally soybean meal or 89% mung beans (high level) and 11% soybean meal. In the last three seasons the level of mung beans in the supplemental protein was reduced to 61% mung beans with 39% soybean meal (moderate level). Feeding the high level of mung beans decreased (P less than .05) weight gain during gestation and reduced (P less than .05) weight loss during lactation compared with gilts fed the control diet or the moderate level of mung beans. Little difference was noted in litter size at birth, but litter size at 21 d for gilts fed moderate levels of mung beans was less (P less than .05) than for gilts fed the control diet or the high level of mung beans. Little difference was noted in survival rate to 21 or 42 d or individual and litter weights at birth and 21 d. Pig and litter weights at 42 d, however were reduced in gilts fed the high level of mung beans (P less than .05 and P less than .10, respectively) compared with the control diet.(ABSTRACT TRUNCATED AT 250 WORDS)

Animal Feed↗
PubMed1998

Tetragonal Crystal Structure of Mung Bean Inhibitor-porcine Trypsin Complex.

Crystal structure of the mung bean inhibitor-porcine trypsin (1:2) ternary complex in the tetragonal crystal with space group I422 was determined at 0.25nm resolution. 56 residues of the mung bean inhibitor were resolved among which one more residue Pro11 was determined than the previously reported structure in the trigonal crystal of the same complex. The structure of the inhibitor in the tetragonal crystal is similar to that in the trigonal crystal and the complexes in tetragonal crystal is also in packing disorder as in trigonal crystal, i.e., the complexes pack in two orientations Ta : MaMb : Tb and Tb : MbMa : Ta(Ta, Tb=trypsin, Ma, Mb=loop I and loop II of mung bean inhibitor respectively). But there are some differences in the two crystal forms. First, the inhibitor in the tetragonal crystal has no pseudo- beta-sheet structure which the trigonal crystal has. Second, its conformation is somewhat different from that in the trigonal crystal.Analysis showed that the linkage peptides between the two regid domains of the inhibitor were flexible, which also accounted for the formation of different crystal forms of this complex. Moreover, comparing mung bean inhibitor to other Bowman-Birk inhibitors showed that the two double-stranded antiparallel beta-sheets and the reactive binding loops were highly conservative.

Journal Article↗
PubMed1995

Activity of single-stranded DNA endonucleases in mung bean is associated with cell division.

A single-strand-specific endonuclease from mung bean sprouts is widely used in molecular biology. However, the biological role of this enzyme is unknown. We studied the spatial and temporal activity of single-stranded DNA endonucleases in mung bean seedling by following enzyme activity that linearizes supercoiled plasmid DNA, a characteristic of this type of enzyme. The formation of a linear molecule from supercoiled DNA was found to occur in two distinguishable steps. The first, which involves introducing a nick into the supercoiled DNA and relaxing it, is very rapid and complete within a few seconds. The second step of cleaving the opposite strand to generate a unit-length linear duplex DNA is a relatively slow process. Analysis of the DNA cleavage sites showed the nuclease preferentially cuts supercoiled DNA at an AT-rich region. Varying levels of nuclease activity could be detected in different tissues of the mung bean seedling. The highest activity was in the root tip and was correlated with histone H1 kinase activity. This implies a link between nuclease activity and cell division. Induction of cell division in mung bean hypocotyls with auxin promoted formation of root primordia and considerably increased the activity of single-stranded DNA endonucleases. The nuclease activity and histone H1 kinase activity were reduced in mung bean cuttings treated with hydroxyurea, but not in cuttings treated with oryzalin. The potential function of single-stranded DNA endonucleases is discussed.

Base Sequence↗
PubMed1999

Disinfection of mung bean seed with gaseous acetic acid.

Mung bean seed inoculated with Salmonella Typhimurium, Escherichia coli O157:H7, and Listeria monocytogenes (3 to 5 log CFU/g) was exposed to gaseous acetic acid in an aluminum fumigation chamber. Salmonella Typhimurium and E. coli O157:H7 were not detected by enrichment of seeds treated with 242 microl of acetic acid per liter of air for 12 h at 45 degrees C. L. monocytogenes was recovered by enrichment from two of 10 25-g seed samples treated in this manner. Fumigation with gaseous acetic acid was also lethal to indigenous bacteria and fungi on mung bean seed. The treatment did not significantly reduce seed germination rates, and no differences in surface microstructure were observed between treated and untreated seed viewed by scanning electron microscopy.

Acetic Acid↗
PubMed1990

Subunit composition of vacuolar membrane H(+)-ATPase from mung bean.

The vacuolar H(+)-ATPase from mung bean hypocotyls was solubilized from the membrane with lysophosphatidycholine and purified by QAE-Toyopearl column chromatography. The purified ATPase was active only in the presence of exogenous phospholipid and was inhibited by nitrate, dicyclohexyl carbodiimide and Triton X-100, but not by vanadate or azide. Dodecyl sulfate/polyacrylamide gel electrophoresis of the purified ATPase yielded ten polypeptides of molecular masses of 68 kDa, 57 kDa, 44 kDa, 43 kDa, 38 kDa, 37 kDa 32 kDa, 16 kDa, 13 kDa and 12 kDa. All polypeptides remained in the peak activity fraction after glycerol density gradient centrifugation. Nine of them, excluding the 43-kDa polypeptide, comigrated in a polyacrylamide gradient gel in the presence of 0.1% Triton X-100. The 16-kDa polypeptide could be labeled with [14C]dicyclohexylcarbodiimide. The amino-terminal amino acid sequence of the isolated 68-kDa polypeptide generally agreed with that deduced from the cDNA for the carrot 69-kDa subunit [Zimniak, L., Dittrich, P., Gogarten, J. P., Kibak, H. & Taiz, L. (1988) J. Biol. Chem. 263, 9102-9112]. Thus, mung bean vacuolar H(+)-ATPase seems to consist of nine distinct subunits.

Amino Acid Sequence↗
PubMed1993

The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin.

The structure of the Bowman-Birk-type inhibitor from mung bean Phaseolus aureus has been determined in ternary complex with porcine trypsin. The complex formed crystals of the trigonal space group P3(1)21 which diffracted to a resolution of 250 pm. Each of the two mung bean protease reactive sites is bound to trypsin according to the standard mechanism for serine proteinase inhibition. The binding loops thereby adopt the canonical conformation for the standard mechanism; however, the sub-van der Waals contact between the active-site serine O gamma (195) and the P1 carbonyl carbon of both loops is significantly smaller (210 pm) than hitherto observed, with continuous electron density connecting the two atoms. The inhibitor is formed by two double-stranded antiparallel beta-sheets, which are connected into a moderately twisted beta-sheet by a network of hydrogen bonds involving main-chain atoms and two water molecules. All contacts with neighbors in the crystal lattice occur between trypsin molecules. This apparently gives rise to an unusual form of disorder where the complexes pack in two orientations Ta:MaMb:Tb and Tb:MbMa:Ta (Ta, Tb = trypsin, Ma = mung bean loop I, Mb = mung bean loop II), such that the asymmetric unit consists of the ternary complex in two orientations, each with half occupancy. This is nearly equivalent to an asymmetric unit which has one trypsin molecule with full occupancy and one mung bean inhibitor with half occupancy and a crystallographic twofold symmetry axis through its center. Because of the approximate twofold symmetry of the inhibitor itself, however, the electron density was interpretable for most of the inhibitor (17 residues at the termini were not resolved) and shows evidence of its double orientation.

Animals↗