{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T15:52:11Z","timestamp":1770911531735,"version":"3.50.1"},"reference-count":42,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2020,3,4]],"date-time":"2020-03-04T00:00:00Z","timestamp":1583280000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,3,4]],"date-time":"2020-03-04T00:00:00Z","timestamp":1583280000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100001501","name":"University Grants Commission","doi-asserted-by":"publisher","award":["F.4-5(107-FRP)\/2014(BSR)"],"award-info":[{"award-number":["F.4-5(107-FRP)\/2014(BSR)"]}],"id":[{"id":"10.13039\/501100001501","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Department of Science and Technology,  IN","award":["ECR\/2016\/000888"],"award-info":[{"award-number":["ECR\/2016\/000888"]}]},{"DOI":"10.13039\/501100010803","name":"Department of Biotechnology","doi-asserted-by":"crossref","award":["BT\/PR-9028\/INF\/22\/193\/2013"],"award-info":[{"award-number":["BT\/PR-9028\/INF\/22\/193\/2013"]}],"id":[{"id":"10.13039\/501100010803","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["3 Biotech"],"published-print":{"date-parts":[[2020,4]]},"DOI":"10.1007\/s13205-020-2140-7","type":"journal-article","created":{"date-parts":[[2020,3,4]],"date-time":"2020-03-04T05:50:56Z","timestamp":1583301056000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Entrapment of enzyme in the presence of proline: effective approach to enhance activity and stability of horseradish peroxidase"],"prefix":"10.1007","volume":"10","author":[{"given":"Rajani","family":"Singh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ambuj Bhushan","family":"Jha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amarendra Narayan","family":"Misra","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2578-8477","authenticated-orcid":false,"given":"Pallavi","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2020,3,4]]},"reference":[{"key":"2140_CR1","doi-asserted-by":"crossref","first-page":"278","DOI":"10.4018\/978-1-5225-5237-6.ch012","volume-title":"Research advancements in pharmaceutical, nutritional, and industrial enzymology","author":"S Agarwal","year":"2018","unstructured":"Agarwal S, Gupta KK, Chaturvedi VK, Kushwaha A, Chaurasia PK, Singh MP (2018) The potential application of peroxidase enzyme for the treatment of industry wastes. In: Bharati SL, Chaurasia PK (eds) Research advancements in pharmaceutical, nutritional, and industrial enzymology. IGI Global, USA, pp 278\u2013293"},{"key":"2140_CR2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BA20010049","volume":"35","author":"E Agostini","year":"2002","unstructured":"Agostini E, Hernandez-Ruiz J, Arnao M, Milrand SR, Tigier HA, Acosta MA (2002) A peroxidase isoenzyme secreted by turnip (Brassica napus) hairy-root cultures: inactivation by hydrogen peroxide and application in diagnostic kits. Biotechnol Appl Biochem 35:1\u20137","journal-title":"Biotechnol Appl Biochem"},{"key":"2140_CR3","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1016\/j.jhazmat.2008.12.026","volume":"166","author":"I Alemzadeh","year":"2009","unstructured":"Alemzadeh I, Nejati S (2009) Phenols removal by immobilized horseradish peroxidase. J Hazard Mater 166:1082\u20131086","journal-title":"J Hazard Mater"},{"key":"2140_CR4","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1007\/s10930-011-9306-4","volume":"30","author":"M Altikatoglu","year":"2011","unstructured":"Altikatoglu M, Basaran Y (2011) Additive effect of dextrans on the stability of horseradish peroxidase. Protein J 30:84\u201390","journal-title":"Protein J"},{"key":"2140_CR5","doi-asserted-by":"publisher","DOI":"10.1155\/2013\/714639","author":"N Bansal","year":"2013","unstructured":"Bansal N, Kanwar SS (2013) Peroxidase(s) in environment protection. Sci World J. https:\/\/doi.org\/10.1155\/2013\/714639","journal-title":"Sci World J"},{"key":"2140_CR6","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.jhazmat.2007.12.008","volume":"156","author":"G Bayramoglu","year":"2008","unstructured":"Bayramoglu G, Ar\u0131ca MY (2008) Enzymatic removal of phenol and p-chlorophenol in enzyme reactor: horseradish peroxidase immobilized on magnetic beads. J Hazard Mater 156:148\u2013155","journal-title":"J Hazard Mater"},{"key":"2140_CR7","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.ijbiomac.2014.12.051","volume":"75","author":"Z Bibi","year":"2015","unstructured":"Bibi Z, Shahid F, Qader SAU, Aman A (2015) Agar\u2013agar entrapment increases the stability of endo-\u03b2-1,4-xylanase for repeated biodegradation of xylan. Int J Biol Macromol 75:121\u2013127","journal-title":"Int J Biol Macromol"},{"key":"2140_CR8","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s10953-015-0291-7","volume":"44","author":"MR Bozorgmehr","year":"2015","unstructured":"Bozorgmehr MR, Monhemi H (2015) How can a free amino acid stabilize a protein? Insights from molecular dynamics simulation. J Sol Chem 44:45\u201353","journal-title":"J Sol Chem"},{"key":"2140_CR9","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1021\/cm020768d","volume":"15","author":"JD Brennan","year":"2003","unstructured":"Brennan JD, Benjamin D, Dibattista EM, Gulcev D (2003) Using sugar and amino acid additives to stabilize enzymes within sol\u2013gel derived silica. Chem Mater 15:737\u2013745","journal-title":"Chem Mater"},{"key":"2140_CR10","doi-asserted-by":"crossref","first-page":"23155","DOI":"10.1039\/C5CP03065J","volume":"17","author":"P Bru\u017adziak","year":"2015","unstructured":"Bru\u017adziak P, Adamczak B, Kaczkowska E, Czub J, Stangret J (2015) Are stabilizing osmolytes preferentially excluded from the protein surface? FTIR and MD studies. Phys Chem Chem Phys 17:23155\u201323164","journal-title":"Phys Chem Chem Phys"},{"key":"2140_CR11","first-page":"3","volume":"10","author":"T Chiong","year":"2014","unstructured":"Chiong T, Lau SY, Khor EH, Danquah MK (2014) Enzymatic approach to phenol removal from wastewater using peroxidases. OA Biotechnol 10:3\u20139","journal-title":"OA Biotechnol"},{"key":"2140_CR12","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1007\/BF00405186","volume":"157","author":"GH Egley","year":"1983","unstructured":"Egley GH, Paul RN Jr, Vaughn KC, Duke SO (1983) Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L. Planta 157:224\u2013232","journal-title":"Planta"},{"key":"2140_CR13","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.enzmictec.2009.08.009","volume":"45","author":"R Fernandez-Lafuente","year":"2009","unstructured":"Fernandez-Lafuente R (2009) Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Technol 45:405\u2013418","journal-title":"Enzyme Microb Technol"},{"key":"2140_CR14","first-page":"1127","volume-title":"Biochemistry","author":"RH Garrett","year":"1999","unstructured":"Garrett RH, Grisham CM (1999) Biochemistry, 2nd edn. Saunders College Publisher, Fort Worth, p 1127","edition":"2"},{"key":"2140_CR15","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1080\/10643380903299491","volume":"41","author":"Q Husain","year":"2011","unstructured":"Husain Q, Ulber R (2011) Immobilized peroxidase as a valuable tool in the remediation of aromatic pollutants and xenobiotic compounds: a review. Crit Rev Environ Sci Technol 41:770\u2013804","journal-title":"Crit Rev Environ Sci Technol"},{"key":"2140_CR16","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1201\/9781351104722-17","volume-title":"Approaches for enhancing abiotic stress tolerance in plants","author":"AB Jha","year":"2019","unstructured":"Jha AB, Sharma P (2019) Regulation of osmolytes syntheses in plants and improvement of abiotic stress tolerance: profiling and counteraction. In: Hasanuzzaman M, Nahar K, Fujita M, Oku H, Islam T (eds) Approaches for enhancing abiotic stress tolerance in plants, 1st edn. CRC Press Taylor and Francis, Boca Raton, pp 311\u2013318","edition":"1"},{"key":"2140_CR17","first-page":"846","volume":"43","author":"E Kalaiarasan","year":"2015","unstructured":"Kalaiarasan E, Palvannan T (2015) Efficiency of carbohydrate additives on the stability of horseradish peroxidase (HRP): HRP-catalyzed removal of phenol and malachite green decolorization from wastewater. Clean (Weinh) 43:846\u2013856","journal-title":"Clean (Weinh)"},{"key":"2140_CR18","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1002\/(SICI)1097-4660(199706)69:2<141::AID-JCTB694>3.0.CO;2-U","volume":"69","author":"J Karam","year":"1997","unstructured":"Karam J, Nicell JA (1997) Potential applications of enzymes in waste treatment. J Chem Technol Biotechnol 69:141\u2013153","journal-title":"J Chem Technol Biotechnol"},{"key":"2140_CR19","doi-asserted-by":"crossref","first-page":"6138","DOI":"10.1021\/la200376f","volume":"27","author":"A Kondyurin","year":"2015","unstructured":"Kondyurin A, Nosworthy NJ, Bilek MMM (2015) Effect of low molecular weight additives on immobilization strength, activity, and conformation of protein immobilized on PVC and UHMWPE. Langmuir 27:6138\u20136148","journal-title":"Langmuir"},{"key":"2140_CR20","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.3390\/molecules23123189","volume":"23","author":"D Kossowska","year":"2018","unstructured":"Kossowska D, Kwak K, Cho M (2018) Do osmolytes impact the structure and dynamics of myoglobin? Molecules 23:3189","journal-title":"Molecules"},{"key":"2140_CR21","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1007\/s11676-017-0524-2","volume":"29","author":"Y Li","year":"2018","unstructured":"Li Y, Zhang L, Fang S et al (2018) Variation of soil enzyme activity and microbial biomass in poplar plantations of different genotypes and stem spacings. J For Res 29:963\u2013972","journal-title":"J For Res"},{"key":"2140_CR22","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1021\/ja01318a036","volume":"56","author":"H Lineweaver","year":"1934","unstructured":"Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56:658\u2013666","journal-title":"J Am Chem Soc"},{"key":"2140_CR23","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1385\/ABAB:104:1:81","volume":"104","author":"A Mahmoudi","year":"2003","unstructured":"Mahmoudi A, Nazari K, Moosavi-Movahedi AA (2003) Effect of Mn(II), Co(II), Ni(II) and Cu(II) on horseradish peroxidase: activation, inhibition and denaturation studies. Appl Biochemi Biotechnol 104:81\u201394","journal-title":"Appl Biochemi Biotechnol"},{"key":"2140_CR24","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.jplph.2005.08.003","volume":"163","author":"S Mishra","year":"2006","unstructured":"Mishra S, Dubey RS (2006) Inhibition of ribonuclease and protease activities in arsenic exposed rice seedlings: role of proline as enzyme protectant. J Plant Physiol 163:927\u2013936","journal-title":"J Plant Physiol"},{"key":"2140_CR25","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1080\/13102818.2015.1008192","volume":"29","author":"NR Mohamad","year":"2015","unstructured":"Mohamad NR, Marzuki NHC, Buang NA, Huyop F, Wahab RA (2015) An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes. Biotechnol Biotechnol Equip 29:205\u2013220","journal-title":"Biotechnol Biotechnol Equip"},{"key":"2140_CR26","doi-asserted-by":"crossref","first-page":"133971","DOI":"10.1016\/j.scitotenv.2019.133971","volume":"696","author":"A Mojiri","year":"2019","unstructured":"Mojiri A, Zhou JL, Ohashi A, Ozaki N, Kindaichi T (2019) Comprehensive review of polycyclic aromatic hydrocarbons in water sources, their effects and treatments. Sci Total Environ 696:133971","journal-title":"Sci Total Environ"},{"key":"2140_CR27","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.ibiod.2006.11.002","volume":"59","author":"PR Moreira","year":"2007","unstructured":"Moreira PR, Almeida-Vara E, Malcata FX, Duarte JC (2007) Lignin transformation by a versatile peroxidase from a novel Bjerkandera sp. strain. Int Biodeterior Biodegr 59:234\u2013238","journal-title":"Int Biodeterior Biodegr"},{"key":"2140_CR28","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.cattod.2016.03.049","volume":"282","author":"SY Na","year":"2017","unstructured":"Na SY, Lee Y (2017) Elimination of trace organic contaminants during enhanced wastewater treatment with horseradish peroxidase\/hydrogen peroxide (HRP\/H2O2) catalytic process. Catal Today 282:86\u201394","journal-title":"Catal Today"},{"key":"2140_CR29","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1007\/s11051-013-2038-y","volume":"15","author":"Y Ni","year":"2013","unstructured":"Ni Y, Li J, Huang Z, He K, Zhuang J, Yang W (2013) Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin. J Nanopart Res 15:2038","journal-title":"J Nanopart Res"},{"issue":"4","key":"2140_CR30","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1104\/pp.75.4.974","volume":"75","author":"LG Paleg","year":"1984","unstructured":"Paleg LG, Stewart GR, Bradbeer JW (1984) Proline and glycine betaine influence protein solvation. Plant Physiol 75(4):974\u2013978","journal-title":"Plant Physiol"},{"key":"2140_CR31","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1110\/ps.9.2.344","volume":"9","author":"D Samuel","year":"2000","unstructured":"Samuel D, Kumar TK, Ganesh G, Jayaraman G, Yang PW, Chang MM, Trivedi VD, Wang SL, Hwang KC, Chang DK, Yu C (2000) Proline inhibits aggregation during protein refolding. Protein Sci 9:344\u2013352","journal-title":"Protein Sci"},{"issue":"2","key":"2140_CR32","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0304-4165(78)90400-2","volume":"541","author":"B Schobert","year":"1978","unstructured":"Schobert B, Tschesche H (1978) Unusual solution properties of proline and its interaction with proteins. BBA-Gen Subj 541(2):270\u2013277","journal-title":"BBA-Gen Subj"},{"key":"2140_CR33","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.plantsci.2004.04.028","volume":"167","author":"P Sharma","year":"2004","unstructured":"Sharma P, Dubey RS (2004) Ascorbate peroxidase from rice seedlings; properties of enzyme isoforms, effects of stress and protective roles of osmolytes. Plant Sci 167:541\u2013550","journal-title":"Plant Sci"},{"key":"2140_CR34","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1016\/j.jplph.2004.09.011","volume":"162","author":"P Sharma","year":"2005","unstructured":"Sharma P, Dubey RS (2005) Modulation of nitrate reductase activity in rice seedlings under aluminium toxicity and water stress: role of osmolytes as enzyme protectant. J Plant Physiol 162:854\u2013864","journal-title":"J Plant Physiol"},{"key":"2140_CR35","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1016\/S0031-9422(98)00282-9","volume":"49","author":"SS Sharma","year":"1998","unstructured":"Sharma SS, Schat H, Voojis R (1998) In vitro alleviation of heavy metal-induced enzyme inhibition by proline. Phytochemistry 49:1531\u20131535","journal-title":"Phytochemistry"},{"key":"2140_CR36","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/0003-9861(92)90257-W","volume":"299","author":"X Shi","year":"1992","unstructured":"Shi X, Dalal S, Kasprzak KS (1992) Generation of free radicals from lipid hydroperoxides by Ni2+ in the presence of oligopeptides. Arch Biochem Biophys 299:154\u2013162","journal-title":"Arch Biochem Biophys"},{"key":"2140_CR37","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1080\/10942912.2016.1247363","volume":"20","author":"S Singh","year":"2017","unstructured":"Singh S, Jha AB, Misra AN, Sharma P (2017) Amorphophallus paeoniifolius corm: a potential source of peroxidase for wide applications. Int J Food Prop 20:2658\u20132664","journal-title":"Int J Food Prop"},{"key":"2140_CR38","doi-asserted-by":"crossref","first-page":"2064","DOI":"10.3390\/molecules24112064","volume":"24","author":"JO Unuofin","year":"2019","unstructured":"Unuofin JO, Okoh AI, Nwodo UU (2019) Aptitude of oxidative enzymes for treatment of wastewater pollutants: a laccase perspective. Molecules 24:2064","journal-title":"Molecules"},{"key":"2140_CR39","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.phytochem.2003.10.022","volume":"65","author":"NC Veitch","year":"2004","unstructured":"Veitch NC (2004) Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 65:249\u2013259","journal-title":"Phytochemistry"},{"key":"2140_CR40","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1016\/j.ijbiomac.2017.08.133","volume":"l106","author":"MB Vineh","year":"2018","unstructured":"Vineh MB, Saboury AA, Poostchi AA, Chi AA, Rashidi AM, Parivar K (2018) Stability and activity improvement of horseradish peroxidase by covalent immobilization on functionalized reduced graphene oxide and biodegradation of high phenol concentration. Int J Biol Macromo l106:1314\u20131322","journal-title":"Int J Biol Macromo"},{"key":"2140_CR41","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0301-4622(96)02222-3","volume":"64","author":"G Xie","year":"1997","unstructured":"Xie G, Timasheff SN (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 64:25\u201343","journal-title":"Biophys Chem"},{"key":"2140_CR42","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1021\/acs.langmuir.8b02001","volume":"35","author":"G Zheng","year":"2019","unstructured":"Zheng G, Liu S, Zha J, Zhang P, Xu X, Chen Y, Jiang S (2019) Protecting enzymatic activity via zwitterionic nanocapsulation for the removal of phenol compound from wastewater. Langmuir 35:1858\u20131863","journal-title":"Langmuir"}],"container-title":["3 Biotech"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s13205-020-2140-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s13205-020-2140-7\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s13205-020-2140-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,4]],"date-time":"2021-03-04T00:53:36Z","timestamp":1614819216000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s13205-020-2140-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,4]]},"references-count":42,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2020,4]]}},"alternative-id":["2140"],"URL":"https:\/\/doi.org\/10.1007\/s13205-020-2140-7","relation":{},"ISSN":["2190-572X","2190-5738"],"issn-type":[{"value":"2190-572X","type":"print"},{"value":"2190-5738","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,3,4]]},"assertion":[{"value":"27 January 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 February 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 March 2020","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"There is no conflict of interest related to this study.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}],"article-number":"155"}}