The multifaceted nature of plant acid phosphatases: purification, biochemical features, and applications

Figures & data

Figure 1. Determination of acid phosphatase activity using (a) p-nitrophenyl phosphate, (b) alpha-naphthyl phosphate, and (c) 4-mrthyllumbelliferyl phosphate substrates.

Figure 2. (a) Native PAGE of rice bean acid phosphatase stained with silver staining showing a single band. (b) Activity-stained gel using Fast Garnet GBC salt and α-naphthyl phosphate. (c) Lane 1 Mobility of silver stained standard molecular mass marker proteins (14.3–97.7 kDa). Lane 2 Denaturing SDS-PAGE of silver stained rice bean acid phosphatase⁵⁵.

Table 1. Biochemical characteristics of acid phosphatases purified from different plant sources.

Enzyme source	Molecular weight	Temp opt	pH opt	Activator	Inhibitor	Ref.
Vigna radiata	Two isoforms ∼29 kDa & ∼18 kDa	50 °C (for 29 kDa isoform)	5.5	Ca, Na	Hg, Cu, Pi, vanadate, Fluoride	^12
thaliana seedlings	Native 100 (Homodimer) Subunits 55 kDa	–	5.6	Mg, Co, Mn, Ba, Mg	Fe^2+, Cu^2+, Zn^2+	^24
Solanum tuberosum tuber	Native 100 kDa Subunits: 55 & 57 kDa	–	5.8	Mg	molybdate, vanadate, and Zn	^29
Cotyledons of Psoralea corylifolia L.	Two isoforms: ∼28 kDa & ∼30 kDa	50 °C	5.5		Cu^2+ , NaF, NaMoO4	^48
Cucurbitaceae seeds	Two isoforms: ∼70 kDa ∼55 kDa	60 °C 55 °C		Mg, K, EDTA	Zn^2+	^49
V. Mungo L. seedlings	25 kDa	55 °C	5.0	K, Cu, Ba	Mg^2+, Zn^2+, EDTA	^50
Cicer arietinum	–	50 °C	5.5	Co^2+, Ca^2+	Zn^2+, Hg^2+	^51
Arachis hypogaea seedlings PI, PIIa & PIIb	PI = 25.3 (heterodimer) Subunits: 14 and 12 kDa PIIa= 22.4 & PIIb = 24 kDa	55 °C	5.0	–	–	^52
Banana Fruit	40 kDa	–	5.8	Mg, Mn	Pi, Mo, vanadate, arsenate,Zn^2+	^56
L. esculentum	Native 142 (heterodimer) Subunits: 63 & 57 kDa	–	5.1	Mg	Zn, Cu, Fe, molybdate, vanadate, fluoride and Pi.	^57
Garlic seedlings	58 kDa	50 °C	5.7	Na, Ca, K	Cu, Mo, Mn	^58
Soybean seeds	51, 58, 52 & 30 kDa for AP1, AP2, AP3A, AP3B isoforms respectively	60 °C for AP1, AP2, AP3B & 50 °C AP3A.	–	–	Pi, Fluoride, Mo, vanadate, Cu, Zn	^59
Carthamus oxyacantha seedlings	36 kDa	50 °C	5.0			^60
Vigna umbellata Thunb.	80 kDa.	60 °C	5.5	–	–	^55
Erythrina indica	89 kDa, two subunits with MW of 38 and 42 kDa	30–50 °C	5	Zn, Hg	Cu, Ca	^54
Opuntia megacantha Salm-Dyck	44 kDa	60 °C	5.5	Ca^2+	Strongly inhibited Cu^2+ and Fe^3+, moderately inhibited by Mg^2+ and Zn^2+. Br^−, CN^−, F^−, I^− and N^3−	^61
Chenopodium murale seedlings	29 kDa	50 °C	5	–	–	^62
Macrotyloma uniflorum seeds	55 kDa, heterodimer of subunits having MW 27 and 28 kDa	50 °C	5	Mg^2+	Strongly inhibited by Hg^2+ moderate inhibition was observed with Ag^+	^43

Figure 3. Stick representation of ADV (magenta carbons) bound to the active site of rkbPAP (light blue carbons). The metal ions are shown as spheres with Fe(III) in yellow, Zn(II) in cyan and Na(I) in purple. Bonds to metal ions are in yellow and hydrogen bonds are in light teal. Water molecules are shown as red spheres. Copyright @ Wiley, Feder et al.¹⁵.

Figure 4. Applications of acid phosphatases.

Nongpiur SR, Kalita T, Belho K, Ambasht PK. purification and partial characterization of acid phosphatase from rice bean (Vigna umbellata thunb.). J Proteins Proteom. 2021;12(4):325–335.

 Google Scholar

Nadir S, Saeed A, Naz R, Siddiqua A, Sherazi M, Wazir SM, Saeed A. Isolation, purification and characterization of acid phosphatase from germinating Vigna radiata seeds. J Chem Soc Pakistan. 2012; 34(3):717–727.

 Web of Science ®Google Scholar

Veljanovski V, Vanderbeld B, Knowles VL, Snedden WA, Plaxton WC. Biochemical and molecular characterization of AtPAP26, a vacuolar purple acid phosphatase up-regulated in phosphate-deprived arabidopsis suspension cells and seedlings. Plant Physiol. 2006;142(3):1282–1293.

 PubMed Web of Science ®Google Scholar

Gellatly KS, Moorhead GBG, Duff SMG, Lefebvre DD, Plaxton WC. Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity. Plant Physiol. 1994;106(1):223–232.

 PubMed Web of Science ®Google Scholar

Satendra S, Luthra PM. Identification, characterization and partial purification of acid phosphatase from cotyledons of Psoralea corylifolia L. Am J Plant Physiol. 2011;6(4):228–241.

 Google Scholar

Koffi DM, Gonnety JT, Faulet BM, Bédikou ME, Kouamé LP, Bi IAZ, Niamké SL. Biochemical characterization of two non-specific acid phosphatases from Cucurbitaceae (Lagenaria Siceraria) edible seeds exhibiting phytasic activity. J Anim Plant Sci. 2010;7:860–875.

 Google Scholar

Asaduzzaman AKM, Rahman HM, Yeasmin T. Purification and characterization of acid phosphatase from a germinating black gram (Vigna Mungo L.) Seedling. Arch Biol Sci. 2011;63(3):747–756.

 Google Scholar

Kaur P, Sharma AD, Rakhra G. Purification and characterization of a heat-stable acid phosphatase from Chickpea. Res Plant Biol. 2011;1(4):1–6.

 Google Scholar

Gonnety JT, Niamké S, Faulet BM, Jean-Parfait E, Kouamé LP. Purification and characterization of three lowmolecular-weight acid phosphatases from Peanut (Arachis Hypogaea) seedlings. African J Biotechnol. 2006;5(1):35–44.

 Web of Science ®Google Scholar

Panara F, Pasqualini S, Antonielli M. Multiple forms of barley root acid phosphatase: purification and some characteristics of the major cytoplasmic isoenzyme. Biochim Biophys Acta. 1990;1037(1):73–80.

 PubMedGoogle Scholar

Guo J, Pesacreta TC. Purification and characterization of an acid phosphatase from the bulb of Allium Cepa L. Var. Sweet Spanish. J Plant Physiol. 1997;151(5):520–527.

 Web of Science ®Google Scholar

Penheiter AR, Duff SMG, Sarath G. Soybean root nodule acid phosphatase. Plant Physiol. 1997;114(2):597–604.

 PubMed Web of Science ®Google Scholar

Bozzo GG, Raghothama KG, Plaxton WC. Structural and kinetic properties of a novel purple acid phosphatase from phosphate-starved tomato (Lycopersicon esculentum) cell cultures. Biochem J. 2004;377(Pt 2):419–428.

 PubMedGoogle Scholar

Bhargava R, Sachar RC. Induction of acid phosphatase in cotton seedlings: enzyme purification, subunit structure and kinetic properties. Phytochemistry. 1987;26(5):1293–1297.

 Google Scholar

Konozy EHE. Purification and characterization of acid phosphatase (AcPase) from cotyledon of Erythrina indica. Glob Adv Res J Agric Sci. 2016;5(6):195–203.

 Google Scholar

Barrett-Lennard EG, Greenway H. Partial separation and characterization of soluble phosphatases from leaves of wheat grown under phosphorus deficiency and water deficit. J Exp Bot. 1982;33(4):694–704.

 Google Scholar

Uehara K, Fujimoto S, Taniguchi T. Isolation of violet-colored acid phosphatase from sweet potato. J Biochem. 1971;70(1):183–185.

 PubMed Web of Science ®Google Scholar

Tagad CK, Sabharwal SG. Purification and characterization of acid phosphatase from Macrotyloma uiflorum seeds. J Food Sci Technol. 2018; 55(1):313–320.

 PubMed Web of Science ®Google Scholar

Feder D, Gahan LR, McGeary RP, Guddat LW, Schenk G. The binding mode of an ADP analogue to a metallohydrolase mimics the likely transition state. ChemBioChem. 2019;20(12):1536–1540.

 PubMed Web of Science ®Google Scholar