Samanta Saptadip; Das Arpan; Haider Suman Kumar; Jana Arijit; Kar Sanjay; Mohapatra Pradeep Kumar Das; Pad Bikash Ranjan; Mondal Keshab Chandra: Thermodynamic and kinetic characteristics of an a-amylase from Bacillus licheniformis SKB4. In: Acta biologica Szegediensis, (58) 2. pp. 147-156. (2014)
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Absztrakt (kivonat)
An amylolytic bacterial strain, Bacillus licheniformis SKB4 produced maximum amylase at pH 6.5 at 42 °C, and at late stationary phase (24 h) of growth. Starch and peptone were found the best supporting carbon and nitrogen source with C:N ratio of 1:2 for amylase production. The purified enzyme was non-responsive to most of the metal ions except K+ and Mg++ (1.0 mM). The enzyme was stable and active at pH 6.5. The enzyme showed optimum temperature at 90 °C with 10 min of half life (t½) at 100 °C. The Q10 of the enzyme was 1.0. The thermodynamic principles like activation energy, free energy for substrate binding and transition state of the enzyme were found 31.53, 5.53 and -17.4 KJ/Mol of starch, respectively. The kinetic constant like Vmax, Km, K catand catalytic efficiency (Kcat/Km)for starch were found to be 1.04 μmol mg-1 min-1, 6.2 mg ml-1,2 × 103 S-1 and 3.22 × 102 ml mg-1 S-1,respectively. All these findings suggested that this amylase has unique characteristics for starch hydrolysis in respect to thermostability and kinetic properties.
Mű típusa: | Cikk, tanulmány, mű |
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Rovatcím: | Articles |
Befoglaló folyóirat/kiadvány címe: | Acta biologica Szegediensis |
Dátum: | 2014 |
Kötet: | 58 |
Szám: | 2 |
ISSN: | 1588-385X |
Oldalak: | pp. 147-156 |
Nyelv: | angol |
Befoglaló mű URL: | http://acta.bibl.u-szeged.hu/39268/ |
Kulcsszavak: | Mikrobiológia |
Megjegyzések: | Bibliogr.: p. 155-156. |
Feltöltés dátuma: | 2016. okt. 17. 10:37 |
Utolsó módosítás: | 2021. ápr. 12. 15:40 |
URI: | http://acta.bibl.u-szeged.hu/id/eprint/34911 |
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