β-galactosidase (EC 184.108.40.206) is important in the formation of a medicinal plant Artemisia judaica (al-ba’atharan) aroma. The crude plant extracts of Artemisia judaica were used to characterize the enzyme in the term of pH, temperature, enzyme kinetic and effects of some heavy metals on its activity. The enzyme activity was measured by its ability to hydrolyze the substrate 2-nitrophenyl β-D-galactopyranoside (ONPG). The enzyme activity was reached maximum at 50°C and at pH 6.0. The Km and Vmax values of the enzyme were 3.6 mM and 1.67 μmol/min, respectively. Uncompetitive inhibition was observed in presence of Hg+2, Fe+3 and Zn+2 for the enzyme β-galactosidase in the crude extract through the decrease in the Km and Vmax values. Pb+2 and Cu+2 were found to act as a noncompetitive inhibitors on the enzyme β-galactosidase in the crude extract due to increase in the Km values and decrease in Vmax values. The study showed that Hg+2 was the most potent inhibitor while Cu+2 exhibited the least inhibition degree on β-galactosidase activity in the Artemisia judaica. These finding indicated that the enzyme β-galactosidase in the crude leaves extract of Artemisia judaica can be used in industrial and medical applications.
Omar M. Atrooz,
Mohammad H. Abukhalil,
Ibrahim M. AlRawashdeh,
Characterization of β-galactosidase in the Crude Plant Extract of Artemisia judaica L. in Presence and Absence of Some Heavy Metals, American Journal of Life Sciences.
Vol. 4, No. 5,
2016, pp. 99-105.
Matthews BW. The structure of E. coli β-galactosidase. Competes Rendus Biologies, 2005, 328 (6): 549-56.
Alliet P Scholtens P Raes M Hensen K Jongen H Rummens JL Boehm G and Vandenplas Y. Effect of prebiotic galacto oligosaccharide, long-chain fructo oligosaccharide infant formula on serum cholesterol and triacylglycerol levels. Nutr, 2007, 23: 719-723.
Pal A Pal V Ramana K V. Extraction and characterization of β - galactosidase from Kluyveromyces lactis NRRL-Y-1104. Ann. Exp. Agric. Allied Sci., 2007, 2: 67–73.
Pal A Pal V Ramana KV Bawa AS. 2009. Biochemical studies of β-galactosidase from Kluyveromyces lactis. J. Food Sci. Technol. 2009, 46: 217–220.
Seddigh S and Bandani A R. Comparison of α and β-galactosidase activity in the three cereal pests, Haplothrips tritici Kurdjumov (Thysanoptera: Phlaeothripidae), Rhopalosiphum padi L. (Hemiptera: Aphididae) and Eurygaster integricep Puton (Hemiptera: Scutelleridae). Mun Ent Zool., 2012, 7: 904–908.
Pal A Lobo M and Khanum F. Extraction, purification and thermodynamic characterization of almond (Amygadalus communis) β-galactosidase for the preparation of delactosed milk. Food Technol and Biotechnol., 2013, 51: 53-61.
Minic Z and Jouanin L. Plant glycoside hydrolases involved in cell wall polysaccharide degradation. Plant Physiol. Biochem., 2006, 44: 435-449.
Pérez-Almeida I and Carpita N C. Las β-galactosidasas y la dinâmica de la pared celular. Interciencia., 2006, 31: 476-482.
Haider T and Husain Q. Hydrolysis of milk/whey lactose by β-galactosidase: A comparative study of stirred batch process and packed bed reactor prepared with calcium alginate entrapped enzyme. Chem Eng Proc Process Intens, 2008b, 48: 576-580.
Shaikh F A Randriantsoa M Withers S G. Mechanistic analysis of the blood group antigen-cleaving endo-beta-galactosidase from Clostridium perfringens. Biochemistry, 2009, 48 (35): 8396-404.
Jokar A and Karbassi A. In-house Production of Lactosehydrolysed Milk by Beta-galactosidase from Lactobacillus bulgaricus. J. Agr. Sci. Tech., 2011, 13: 577-584.
Hsu, C. A., Yu, R. C., and Chou, C. Production of betagalactosidase by Bifidobacteria as influenced by various culture conditions. Int J Food Microbiol., 2005, 104: 197–206.
Heyman M B. Lactose intolerance in infants, children, and adolescents. Pediatrics, 2006, 118: 1279–1286.
Neri D F Balcao VM Carneiro-da-Cunha M G Carvalho JR LB Teixeira JA. Immobilization of β-galactosidase from Kluyveromyces lactis onto a polysiloxane-polyvinyl alcohol magnetic (mPOS-PVA) composite for lactose hydrolysis. Catal Comm., 2008, 4: 234–239.
Husain Q. β-Galactosidases and their potential applications: a review. Crit. Rev. Biotechnol., 2010, 30: 41-62.
Seddigh S and Darabi M. Comprehensive analysis of bet-agalactosidase protein in plants based on Arabidopsis thaliana. Turk J Biol., 2014, 38: 140-150.
Kishore D and Kayastha AM. A β-galactosidase from chick pea (Cicer arietinum) seeds: Its purification, biochemical properties and industrial applications. Food Chemistry, 2012, 13: 1113–1122.
Gulzar S and Amin S. Kinetic Studies on β-Galactosidase Isolated from Apricots (Prunus armeniaca kaisa). American Journal of Plant Sciences, 2012, 3: 636-645.
Sudério F B Barbosa G K Gomes-Filho E and Enéas-Filho J. Purification and characterization of cytosolic and cell wall β-galactosidases from Vigna unguiculata stems. Braz. J. Plant Physiol., 2011, 23 (1): 5-14.
Yossef HD and El Beltagey AE. Extraction, purification and characterization of apricot Seed β-Galactosidase for Producing Free Lactose Cheese. J Nutr Food Sci., 2014, 4: 270.
Chantarangsee M Fujimura T Fry S C Ketudat-Cairns J R. Molecular characterization of β-galactosidases from germinating rice (Oryza sativa). Plant Sci., 2007, 173: 118-134.
Ogasawara, S., Abe, K., and Nakajima, T. Pepper beta-galactosidase 1 (PBG1) plays a significant role in fruit ripening in bell pepper (Capsicum annuum). Biosci. Biotechnol. Biochem., 2007, 71 (2): 309-22.
Dean G H Zheng H Tewari J Huang J Young D S Hwang Y T Western T L Carpita N C McCann M C Mansfield S D Haughna G W. The Arabidopsis MUM2 Gene Encodes a β-Galactosidase Required for the Production of Seed Coat Mucilage with Correct Hydration Properties. The Plant Cell, 2007, 19: 4007–4021.
Zhuang, J. P., Su, J., Li, X. P., and Chen, W. X. Cloning and expression analysis of β-Galactosidase gene related to softening of banana (Musa sp.) Fruit. Journal of Plant. Physiology and Molecular Biology, 2006, 32 (4): 411-419.
Figueiredo, S. A., Lashermes, P., and Aragão, F. J. Molecular characterization and functional analysis of the β-galactosidase gene during Coffea arabica (L.) fruit development. J Exp Bot., 2011, 62 (8): 2691-703.
Hruba P Honys D Twell D Capková V and Tupy J. Expression of β-Galactosidase and β-Xylosidase Genes during Microspore and Pollen Development. Planta, 2005, 220 (6): 931-940.
Wu, A., and Liu, J. Isolation of the Promoter of a Cotton β- galactosidase Gene GhGall and Its Expression in Transgenic Tobacco Plants. Science in China Series C: Life Sciences, 2006, 49 (2): 105-114.
Iglesias N Abelenda JA Rodino M Sampedro J Revilla G and Zarra I. Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana. Plant and Cell Physiology, 2006, 47: 55-63.
Martin I Jimenez T Esteban R Dopico B and Labrador E. Immunolocalization of a cell wall β-galactosidase reveals its developmentally regulated expression in Cicer arietinum and its relationship to vascular tissue. J. Plant Growth Regul., 2008, 27: 181-191.
Dwevedi, A., & Kayastha, A. M. Plant β-Galactosidases: Physiological Significance and Recent Advances in Technological Applications. J. Plant Biochemistry and Biotechnology, 2010, 19 (1): 09-20.
Aldoobie NF and Beltagi MS. Physiological, biochemical and molecular responses of common bean (Phaseolus vulgaris L.) plants to heavy metals stress. African Journal of Biotechnology, 2013, 12 (29): 4614- 4622.
Gaur A and Adholeya A. Prospects of arbuscular mycorrhizal fungi in phytoremediation of heavymetal contaminated soils. Current Science., 2004, 86 (4): 528–534.
Goyer R A. Toxic and essential metal interactions. Annu Rev Nutr., 1997, 17: 37-50.
Nedelkoska TV and Doran PM. Characteristics of heavy metal uptake by plant species with potential for phytoremediation and phytomining. Miner. Eng., 2000, 13: 549–561.
Schützendübel A and Polle A. Plant responses to abiotic stress: heavy metal induced oxidative stress and protection by mycorrhization. J Exp Bot., 2002, 53: 1351-1365.
Nofal SM Mahmoud SS Ramadan A Soliman GA and Fawzy R. Anti- Diabetic effect of Artemisia judaica extracts. Res. J. Med. Med. Sci. 2009, 4 (1): 42–48.
Al-Rawashdeh IM. Genetic variability in a medicinal plant Artemisia judaica using random amplified polymorphic DNA (RAPD) Markers. Int. J. Agric. Biol., 2011, 13: 279–282.
Abd-Elhady HK. Insecticidal activity and chemical composition of essential oil from Artemisia judaica L. against Callosobruchus maculatus (F.) (coleoptera: bruchidae). J. Plant Prot. Res., 2012, 52 (3): 347- 352.
Abou El-Hamd HM El-Sayed MA Hegazy ME Helaly SE Abeer ME and Naglaa SM. Chemical constituents and biological activities of Artemisia herba-alba. Rec Nat Prod., 2010, 4: 1-25.
Tilaoui M Mouse HA Jaafari A Aboufatima R Chait A and Zyad A. Chemical composition and antiproliferative activity of essential oil from aerial parts of a medicinal herb Artemisia herba-alba. Rev. Bras. Farmacogn., 2011, 21 (4): 781-785.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. Protein measurement with the Folin phenol reagent. J Biol Chem., 1951, 193: 265–275.
Sekimata M Ogura K Tsumuraya Y Hashimoto Y and Yamamoto S. A β -Galactosidase from Radish (Raphanus sativus L.) Seeds. Plant Physiol., 1989, 90: 567-574.
Lineweaver, H., and Burk, D. The determination of enzyme dissociation constants. J. Am. Chem. Soc., 1934, 56: 658–666.
Talwar G. P. and Srivastava L. M. Textbook of biochemistry and human biology, 2006, 3rd Ed. Prentice-Hall: New Delhi.
McGee CM and Murray DR. Comparative-studies of acid 3 glycosidases from legumes. Annals of Botany, 1986, 57: 179–190.
Lee DH Kang SG Suh SG and Byun JK. Purification and characterization of a beta-galactosidase from peach (Prunus persica). Mol Cells, 2003, 15: 68-74.
Alcântara PH Martim L Silva CO Dietrich SM Buckeridge MS. Purification of a β-galactosidase from cotyledons of Hymenaea courbaril L. (Leguminosae). Enzyme properties and biological function. Plant Physiol Biochem., 2006, 44: 619-627.
Biswas S Kayastha AM and Seckler R. Purification and characterization of a thermo stable β-galactosidase from kidney beans (Phaseolus vulgaris L.) cv. PDR14. Journal of Plant Physiology, 2003, 160: 327–337.
Richard A. Harvey and Denise R. Ferrier. Lippincott’s Illustrated Reviews: Biochemistry, Fifth Edition. Lippincott Williams & Wilkins, a Wolters Kluwer business, 2011.
Haider T and Husain Q. Preparation of lactose free milk by using salt fractionated almond (Amygadalus Communis) β -galactosidase. J Sci Food Agric., 2007, 87: 1278-1283.
Edwards M Bowman YJ Dea IC and Reid JS. A β-galactosidase from nasturtium (Tropaeolum majus L.) cotyledons. Purification, properties and demonstration that xyloglucan is the natural substrate. J. Biol. Chem., 1988, 263: 4333–4337.
Li SC Han JW Chen KC and Chen CS. Purification and characterization of isoforms of β-galactosidases in mung bean seedlings. Phytochemistry, 2001, 57: 349–359.
Enéas-Filho J da Costa Barbosa GK Suderio FB Prisco JT and Gomes-Filho E. Isolation and partial purification of β-galactosidases from cotyledons of two cowpea cultivars. Rev. Bras. Fisiol. Veg., 2001, 13: 251–261.
Davies, G., Henrissat, B. Structures and mechanisms of glycosyl hydrolases. Structure, 1995, 3, 853-85.
Shengwen Shen, Xing-Fang Li, William R. Cullen, Michael Weinfeld, and X. Chris Le. Arsenic Binding to Proteins. Chem. Rev., 2013, 113 (10): 7769–7792.
Konno H., and Tsumuki H. Purification of a β-galactosidase from rice shoots and its involvement in hydrolysis of the natural substrate in cell walls. Physiol plant, 1993, 89: 40-47.
Carrington CM and Pressey R. β-Galactosidase II activity in relation to changes in cell wall Galactosyl composition during tomato ripening. Journal of the American Society for Horticultural Science, 1996, 121: 132-136.
Voet D. and Voet J. G. Biochemistry text chapter on Rate of Enzymatic Reactions. 2011, pp. 482-500. Fourth edition. USA: Ed. John Wiley & Sons, Inc.
Baritaux, O., Amiot, M. J., Richard, H. and Nicolas, J. Enzymatic browning of basil (Ocimum basilicum L.) studies on phenolic compounds and polyphenoloxidase. Sciences des Aliments, 1991, 11: 49-62.
Suginta W and Svasti MR. Purif ication and properties of β-galactosidase from Hibiscus sabdariffa L. var. altissima. J. Sci. Soc. Thailand., 1995, 21: 183-186.