title: Nanotechnology enabled enhancement of enzyme activity and thermostability: study on impaired pectate lyase from attenuated Macrophomina phaseolina in presence of hydroxyapatite nanoparticle.
abstract: In this paper we show that hydroxyapatite nanoparticles (NP) can not only act as a chaperon (by imparting thermostability) but can serve as a synthetic enhancer of activity of an isolated extracellular pectate lyase (APL) with low native state activity. The purified enzyme (an attenuated strain of Macrophomina phaseolina) showed feeble activity at 50°C and pH 5.6. However, on addition of 10.5 µg/ml of hydroxyapatite nanoparticles (NP), APL activity increased 27.7 fold with a 51 fold increase in half-life at a temperature of 90°C as compared to untreated APL. The chaperon like activity of NP was evident from entropy-enthalpy compensation profile of APL. The upper critical temperature for such compensation was elevated from 50°C to 90°C in presence of NP. This dual role of NP in enhancing activity and conferring thermostability to a functionally impaired enzyme is reported for the first time.
authors.affiliation: Department of Biochemistry, University of Calcutta, Kolkata, India.
authors.forename: Nalok
authors.initials: N
authors.lastname: Dutta
authors.forename: Arka
authors.initials: A
authors.lastname: Mukhopadhyay
authors.forename: Anjan Kr
authors.initials: AK
authors.lastname: Dasgupta
authors.forename: Krishanu
authors.initials: K
authors.lastname: Chakrabarti
mesh_terms: D000595:Amino Acid Sequence; D001203:Ascomycota / Q000201:enzymology*; D002942:Circular Dichroism; D017886:Durapatite / Q000737:chemistry*; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D053758:Nanoparticles; D036103:Nanotechnology; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
chemical_list: D017886:Durapatite; D011133:Polysaccharide-Lyases; C023911:pectate lyase