Ghosh Priyanka; Das Arpan; Gayen Soumi; Mondal Keshab Chandra; Ghosh Uma: Statistical optimalization of α-Amylase production from Penicillium notatum NCIM 923 and kinetics study of the purified enzyme. In: Acta biologica Szegediensis, (59) 2. pp. 179-188. (2015)
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Absztrakt (kivonat)
In this study, response surface methodology (RSM) was employed to optimize the production of α-amylase by Penicillium notatum NCIM 923 through solid-state fermentation. The individual and combinational effects of the factors, i.e. substrate amount, initial moisture, fermentation time, temperature and size of inoculum were found to have significant effects on α-amylase production: the optimum values of the tested variables were 5 g, 70%, 94 h, 28 °C and 20%, respectively. The predicted amylase production (2819.24 U/g) was in good agreement with the value measured under optimized surrounding (2810.33 U/g). The molecular mass of purified α-amylase was about 52 kDa. The enzyme activity exhibited its pH optimum between pH 4.6 and 6.6, and it had maximal activity at 50 °C. The apparent Km and Vmax of α-amylase for starch were 4.1 mg/ml and 247.6 μmol/min, respectively. The activation energy (Ea) for starch hydrolysis was found to be 14.133 kJ/mol. The enzyme was thermostable with half-life (t1/2) of 110 min at 80 °C and temperature coefficient (Q10) value of 1.0. Purified enzyme was activated by Ca2+ and inhibited by Hg2+ ions. EDTA also inhibited the enzyme activity, indicating that the purified enzyme is a metalloenzyme.
Mű típusa: | Cikk, tanulmány, mű |
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Rovatcím: | Articles |
Befoglaló folyóirat/kiadvány címe: | Acta biologica Szegediensis |
Dátum: | 2015 |
Kötet: | 59 |
Szám: | 2 |
ISSN: | 1588-385X |
Oldalak: | pp. 179-188 |
Nyelv: | angol |
Befoglaló mű URL: | http://acta.bibl.u-szeged.hu/39273/ |
Kulcsszavak: | Penicillium, Mikrobiológia gombák |
Megjegyzések: | Bibliogr.: p. 187-188. |
Feltöltés dátuma: | 2016. okt. 17. 10:36 |
Utolsó módosítás: | 2021. ápr. 12. 15:10 |
URI: | http://acta.bibl.u-szeged.hu/id/eprint/35992 |
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