Isolation and enzymatic properties of a nonspecific acid phosphatase from <i>Vigna aconitifolia</i> seeds

Anand, Akash; Srivastava, Pramod K.

doi:10.1002/bab.1131

Cited by 4 publications

(9 citation statements)

References 43 publications

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“…reports of acid phosphatase isolation from plants describe either a low molecular weight enzyme of around 30 kDa (Zaman et al, 2020;Saeed et al, 2014;Nadir et al, 2012;Asaduzzaman et al, 2011;Zaman et al, 2020) or a higher molecular weight enzyme around 60 kDa (Anand and Srivastava, 2014;Xie and Shang, 2018). This study produced a low molecular weight AP enzyme.…”

Section: Purification Of Acid Phosphatasementioning

confidence: 62%

Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

Lightle¹,

Fosco²,

Giles³

et al. 2021

Afr. J. Biotechnol.

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Acid phosphatase from mung bean (Vigna radiata) germinated seeds was partially purified via ammonium sulfate precipitation and fully purified via gel excision and heat denaturation, yielding a 29 kDa protein. Using 4-nitrophenylphosphate as a substrate, V max and K m values of 0.10 µmol/min and 0.27 mM, respectively, were obtained. The acid phosphatase was heat resistant, enhanced by the presence of Fe 2+ and Mn 2+ salts, and inhibited by the presence of citrate. Mung bean acid phosphatase reacted immunologically with primary antibodies against Solanum tuberosum acid phosphatase, while polymerase chain reaction (PCR) analyses suggest there are some common sequences between mung bean acid phosphatase DNA and that of Arabidopsis thaliana acid phosphatase vegetative storage protein. This suggests plant acid phosphatases are structurally as well as functionally related.

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Section: Purification Of Acid Phosphatasementioning

confidence: 62%

Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

Lightle¹,

Fosco²,

Giles³

et al. 2021

Afr. J. Biotechnol.

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“…Acid phosphatase from Vigna aconitifolia seeds was purified according to Anand et al [20] All chemicals used in experiments were of analytical grade. Chloride and sulfate salts for all metal ions (FeCl 3 , ZnCl 2 , MnCl 2 , CuSO 4 , FeSO4), NaH 2 PO 4 , (NH 4 ) 6 Mo 7 O 24 , and NaF were from either Sisco Research Laboratories Pvt.…”

Section: Methodsmentioning

confidence: 99%

The Inhibitory Effect of Metals and Other Ions on Acid Phosphatase Activity FromVigna aconitifoliaSeeds

Srivastava¹,

Anand²

2014

Preparative Biochemistry and Biotechnology

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Sensitivity of acid phosphatase from Vigna aconitifolia seeds to metal ions, fluoride, and phosphate was examined. All the effectors had different degree of inhibitory effect on the enzyme. Among metal ions, molybdate and ferric ion were observed to be most potent inhibitors and both exhibited mixed type of inhibition. Acid phosphatase activity was inhibited by Cu2+ in a noncompetitive manner. Zn and Mn showed mild inhibition on the enzyme activity. Inhibition kinetics analysis explored molybdate as a potent inhibitor for acid phosphatase in comparison with other effectors used in this study. Fluoride was the next most strong inhibitor for the enzyme activity, and caused a mixed type of inhibition. Phosphate inhibited the enzyme competitively, which demonstrates that inhibition due to phosphate is one of the regulatory factors for enzyme activity.

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“…Co 2+ , Mn 2+ , Fe 3+ , and Cu 2+ inhibited the enzyme at the two p-NPP concentrations (0.1 and 0.5 mM). Mn 2+ ions inhibited some APases (Sugiura et al, 1981;Guo & Pesacreta, 1997;Yenigun & Guvenilir, 2003;Garcia et al, 2004;Anand & Srivastava, 2013). Fe 3+ also inhibited APase isoforms from Vigna species (V. sinensis and V. aconitifolia) and Opuntia (Biswas & Cundiff, 1991;Biswas et al, 1996;Anand & Srivastava, 2013;Chafik, 2020).…”

Section: A Effect Of Cationsmentioning

confidence: 99%

“…Acid phosphatase (EC 3.1.3.2) (APase) catalyzes the hydrolysis of phosphate esters to yield alcohol and inorganic phosphate at pH below 7.0 (Duff et al, 1994). APase got isolated and characterized from different plant sources (Roknabadi et al, 1999;Turner & Plaxton, 2001;Koffi et al, 2010;Anand & Srivastava, 2013;Tagad & Sabharwal, 2018;Zaman et al, 2020;Chafik et al, 2020;Nongpiur et al, 2021). Reports are there on the influence of ions (cations and anions) and metabolites (effectors) on the acid phosphatase activity (Guo & Roux, 1995;Turner & Plaxton, 2001;Coello, 2002;Greiner & Jany, 2003;Koffi et al, 2010;Nadir et al, 2012;Khan et al, 2016;Chafik, 2020).…”

Section: Introductionmentioning

confidence: 99%

“…A similar activation effect was noticed in the coleoptiles and seeds of barley and Lagenaria siceraria APase (Pasqualini et al, 1992;Koffi et al, 2010). Among the metal ions, a study was on the use of Zn 2+ , Cu 2+ , Fe 3+ , Mg 2+ , Mn 2+ , and Ca 2+ (Biswas & Cundiff, 1991;Kawarasaki et al, 1996;Garcia et al, 2004;Senna et al, 2006;Asaduzzaman et al, 2011;Anand & Srivastava, 2013;Khan et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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Rice Bean (Vigna umbellata Thunb.) Acid Phosphatase: Effect of Metal Ions and Metabolites

Nongpiur,

Ambasht

2022

JSR

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Rice bean acid phosphatase dialyzed against ethylenediaminetetracetic acid (1 mM), yielded no loss in activity at 0.5 mM p-nitrophenylphosphate. It had a mild activating effect at 0.1 mM p-nitrophenylphosphate. Divalent cations belonging to group II of Periodic Table like Mg2+, Ca2+, Sr2+, and Ba2+ at 0.5 mM concentration p-nitrophenylphosphate did not affect the enzyme activity. At 0.1 mM p-nitrophenylphosphate, however, only Mg2+ ions showed little inhibition. The transition metal ions viz. Zn2+ , Cu2+, Co2+, Mn2+ and Fe3+ showed inhibition at both pnitrophenylphosphate concentrations. Na+ , K+ , and NH4 + ions did not influence the enzyme activity, but Li+ inhibited the activity at 0.1 and 0.5 mM p-nitrophenylphosphate concentrations, respectively. Molybdate and phosphate anions proved to be strong inhibitors, but vanadate, a moderate inhibitor. Tartrate anion did not exhibit an effect on rice bean acid phosphatase. Sugars, plant hormones, medicines, vitamins, and amino acids at 1.0 mM concentration did not affect the enzyme activity. NADH exhibited the maximum activation, followed by citric acid, isocitrate, and oxaloacetate. Caffeine showed activation in the enzyme activity. Phosphate esters (1-Naphthylphosphate, phenylphosphate, PEP, and ADP) exhibited competitive inhibition when pnitrophenylphosphate was used as a substrate. Non-ionic detergents Triton X-100 and Tween-20 brought activation to the enzyme. The ionic detergent SDS brought complete loss to the enzyme activity. Dithiothreitol brought inhibition to the enzyme activity. The presence of β-mercaptoethanol did not influence the enzyme activity.

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Isolation and enzymatic properties of a nonspecific acid phosphatase from Vigna aconitifolia seeds

Cited by 4 publications

References 43 publications

Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

Vigna radiata (mung bean) acid phosphatase is difficult to purify and may have a role as a vegetative Storage protein

The Inhibitory Effect of Metals and Other Ions on Acid Phosphatase Activity FromVigna aconitifoliaSeeds

Rice Bean (Vigna umbellata Thunb.) Acid Phosphatase: Effect of Metal Ions and Metabolites

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