Abstract
With the aid of experimental design, in this study, we have investigated the activity and stability of dextranase, an important extracellular inducible enzyme that specifically hydrolyzes the α-1,6 glycosidic linkages of dextran, leading to the formation of D-glucose and shorter oligosaccharides. The experimental design results showed the significant individual as well as interaction effects of the tested parameters affecting the dextranase activity and stability. The numerical optimization study suggested that the desired maximum activity and stability of dextranase can be obtained at temperature 40 °C and pH value 6.5. In addition, stability tests showed that dextranase was stable, without compromising its activity, up to 55 °C and in pH range 5–8. Considering the influence of investigated reagents on dextranase activity, the results revealed a pronounced activating effect of glycerol and sucrose, especially with increasing their concentration, with the highest activity detected in the presence of sucrose at 10 mM (129%). Regarding the influence of added metal ions, the higher dextranase activity is recorded in the presence of Ag+, Ca2+, K+, Mg2+, and Si2+ ions, from which the Ca2+ ions were the most effective, and in their presence, at 10 mM the activity of dextranase was 119%.
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References
Abdallah MMS, Abdelgawad ZA, El-Bassiouny HMS (2016) Alleviation of the adverse effects of salinity stress using trehalose in two rice varieties. S Afr J Bot 103:275–282. https://doi.org/10.1016/j.sajb.2015.09.019
Abdel-Naby MA, Ismail AS, Abdel-Fattah AM, Abdel-Fattah AF (1999) Preparation and some properties of immobilized Penicillium funiculosum 258 dextranase. Process Biochem 34:391–398. https://doi.org/10.1016/S0032-9592(98)00127-7
Adeleke R, Dames JF (2014) Kalaharituber pfeilii and associated bacterial interactions. S Afr J Bot 90:68–73. https://doi.org/10.1016/j.sajb.2013.10.003
Bailey EJ, Ollis FD (1986) Biochemical engineering fundamentals. McGraw-Hill Book Co, New York
Bradbury SL, Jakoby WB (1972) Glycerol as an enzyme-stabilizing agent: effects on aldehyde dehydrogenase. Proc Natl Acad Sci USA 69:2373–2376
El-Tanah AB, El-Baz E, Sherief AA (2011) Properties of Aspergillus subolivaceus free and immobilized dextranase. Eur Food Res Technol 233:735–742. https://doi.org/10.1007/s00217-011-1570-1
Erhardt FA, Jördening H (2007) Immobilization of dextranase from Chaetomium erraticum. J Biotechnol 131:440–447. https://doi.org/10.1016/j.jbiotec.2007.07.946
Erhardt FA, Stammen S, Jördening H (2008) Production, characterization and (co-) immobilization of dextranase from Penicillium aculeatum. Biotechnol Lett 30:1069–1073. https://doi.org/10.1007/s10529-008-9659-8
Gerlsma SY, Stuur ER (1972) The effect of polyhydric and monohydric alcohols on the heat-induced reversible denaturation of lysozyme and ribonuclease. Int J Peptide Protein Res 4:377–383. https://doi.org/10.1111/j.1399-3011.1972.tb03444.x
Gerlsma SY, Stuur ER (1974) The effects of combining two different alcohol on the heat-induced reversible denaturation of ribonuclease. Int J Peptide Protein Res 6:65–74. https://doi.org/10.1111/j.1399-3011.1974.tb02362.x
Hild E, Brumbley SM, O’Shea MG, Nevalainen H, Bergquist PL (2007) A Paenibacillus sp. dextranase mutant pool with improved thermostability and activity. Appl Microbiol Biotechnol 75:1071–1078. https://doi.org/10.1007/s00253-007-0936-6
Hoch S (1973) Tryptophan synthetase from bacillus subtilis: purification and characterization of the α-component. J Biol Chem 248:2999–3003. https://doi.org/10.1016/S0021-9258(19)44000-3
Jarabak J (1972) Human placental 15-hydroxyprostaglandin dehydrogenase. Proc Natl Acad Sci USA 69:533–534. https://doi.org/10.1073/pnas.69.3.533
Jarabak J, SeedsJr AE, Talalay P (1966) Reversible cold inactivation of a 17β-hydroxysteroid dehydrogenase of human placenta: protective effect of glycerol. Biochemistry 5:1269–1278. https://doi.org/10.1021/bi00868a021
Jenkins HDB, Marcus Y (1995) Viscosity B-coefficients of ions in solution. Chem Rev 95:2695–2724. https://doi.org/10.1021/cr00040a004
Jiménez ER (2009) Dextranase in sugar industry: a review. Sugar Tech 11:124–134
Khalikova E, Susi P, Usanov N, Korpela T (2003) Purification and properties of extracellular dextranase from a Bacillus sp. J Chromatogr B 796:315–326. https://doi.org/10.1016/j.jchromb.2003.08.037
Khalikova E, Susi P, Korpela T (2005) Microbial dextran hydrolyzing enzymes: fundamentals and applications. Microbiol Mol Biol Rev 69:306–324. https://doi.org/10.1128/MMBR.69.2.306-325.2005
Koenig D, Day D (1989) The purification and characterization of a dextranase from Lipomyces starkeyi. Eur J Biochem 183:161–167. https://doi.org/10.1111/j.1432-1033.1989.tb14908.x
Lee CJ, Timasheff NS (1981) The Stabilization of proteins by sucrose. J Biol Chem 256:7193–7201. https://doi.org/10.1016/S0021-9258(19)68947-7
Madhu GL, Prabhu KA (1984) Studies on dextranase from Penicillium aculeatmn. Enzyme Microb Technol 6:217–220. https://doi.org/10.1016/0141-0229(84)90107-8
Myers JS, Jakoby WB (1973) Effect of polyhydric alcohols on kinetic parameters of enzymes. Biochem Biophys Res Commun 51:631–636. https://doi.org/10.1016/0006-291X(73)91361-2
Ren W, Cai R, Yan W, Lyu M, Fang Y, Wang S (2018) Purification and characterization of a biofilm-degradable dextranase from a marine bacterium. Mar Drugs 15:1–16. https://doi.org/10.3390/md16020051
Ruwart MJ, Suelter CH (1971) Activation of yeast pyruvate kinase by natural and artificial cryoprotectants. J Biol Chem 246:5990–5993
Šmelcerović A, Knežević-Jugović Z, Petronijević Ž (2008) Microbial polysaccharides and their derivatives as current and prospective pharmaceuticals. Curr Pharm Des 14:3168–3195. https://doi.org/10.2174/138161208786404254
Snell F, Snell C (1953) Colorimetric methods analysis. Van Nostrand Co Inc, Totonto
Staat RH, Schachtele CF (1976) Analysis of the dextranase activity produced by an oral strain of Bacteroides ochraceus. J Dent Res 55:1103–1110. https://doi.org/10.1177/00220345760550061701
Sugiura M, Ito A, Ogiso T, Kato K, Asano H (1973) Purification of dextranase from Penicillium funiculosum and its enzymatic properties. Biochim Biophys Acta 309:357–362. https://doi.org/10.1016/0005-2744(73)90034-X
Tekman B, Ozdemir H, Senturk M, Ciftci M (2008) Purification and characterization of glutathione reductase from rainbow trout (Oncorhynchus mykiss) liver and inhibition effects of metal ions on enzyme activity. Comp Biochem Phys C 148:117–121. https://doi.org/10.1016/j.cbpc.2008.04.005
Vagenende V, Yap MG, Trout BL (2009) Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry 48:11084–11096. https://doi.org/10.1021/bi900649t
Wang D, Lu M, Wang X, Jiao Y, Fang Y, Liu Z, Wang S (2014) Improving stability of a novel dextran-degrading enzyme from marine Arthrobacter oxydans KQ11. Carbohyd Polym 103:294–299. https://doi.org/10.1016/j.carbpol.2013.12.025
Wu D, Zhang H, Huang L, Hu X (2011) Purification and characterization of extracellular dextranase from a novel producer, Hypocrea lixii F1002, and its use in oligodextran production. Process Biochem 46:1942–1950. https://doi.org/10.1016/j.procbio.2011.06.025
Wynter CVA, Chang M, De Jersey J, Patel B, Inkerman PA, Hamilton S (1997) Isolation and characterization of a thermostable dextranase. Enzyme Microb Technol 20:242–247. https://doi.org/10.1016/S0141-0229(96)00118-4
Zhang M, Yanming F, Ji Y, Jiang Z, Wang L (2013) Effects of salt stress on ion content, antioxidant enzymes and protein profile in different tissues of Broussonetia papyrifera. S Afr J Bot 85:1–9. https://doi.org/10.1016/j.sajb.2012.11.005
Zhang YQ, Li RH, Zhang HB, Wu M, Hu XQ (2017) Purification, characterization, and application of a thermostable dextranase from Talaromyces pinophilus. J Ind Microbiol Biot 44:1–11. https://doi.org/10.1007/s10295-016-1886-8
Zhao H (2005) Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids. J Mol Catal B-Enzymatic 37:16–25. https://doi.org/10.1016/j.molcatb.2005.08.007
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Republic of Serbia—Ministry of Education, Science and Technological Development, Program for Financing Scientific Research Work, ev. no. 451-03-68/2022-14/200133.
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SS: Conceptualization, Methodology, Validation, Formal analysis, Investigation, Writing—Original Draft, Visualization, SS: Software, Writing—Original Draft, Visualization, SP: Conceptualization, Methodology, Validation, Formal analysis, Investigation, Writing—Original Draft, ZP: Resources, Writing—Original Draft, Visualization.
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Savic, S., Savic, S., Petrovic, S. et al. Activity and Stability of Dextranase from New Penicillium Funiculosum TFZ.91: Optimization by Response Surface Methods. Iran J Sci Technol Trans Sci 46, 747–760 (2022). https://doi.org/10.1007/s40995-022-01293-7
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DOI: https://doi.org/10.1007/s40995-022-01293-7