Critical importance of moisture content of the medium in alpha-amylase production by Bacillus licheniformis M27 in a solid-state fermentation system

1990 ◽  
Vol 33 (5) ◽  
Author(s):  
M.V. Ramesh ◽  
B.K. Lonsane
2018 ◽  
Vol 43 (3) ◽  
pp. 240-247 ◽  
Author(s):  
Nurullah Akcan

AbstractObjective:The aim of this work was to study the optimal cultivation conditions for β-galactosidase production byBacillus licheniformisATCC 12759.Materials and methods:The screening of β-galactosidase production fromB. licheniformisATCC 12759 was performed by solid state fermentation method on media rich with rice bran (RB). Different factors were tested for the optimization of β-galactosidase production.Results:Certain fermentation parameters involving incubation time, incubation temperature, inoculum level, moisture content, initial pH, agitation speed, size of fermentation medium and optimum temperature of β-galactosidase activity were studied separately. Maximal amount of β-galactosidase production was obtained when solid-state fermentation (SSF) was carried out using RB, having inoculum level 35%, moisture content of 20%, initial pH 7.5 at 37°C for 48 h.Conclusion:Results indicated that optimal fermentation conditions play a key role in the maximum production of β-galactosidase fromB. licheniformisATCC 12759. This study shows the potential of the studied enzymes to be promoting candidates for the degradation of lactose and production of important bioproducts.


2005 ◽  
Vol 36 (7) ◽  
pp. 900-902 ◽  
Author(s):  
Yovita S.P. Rahardjo ◽  
Frans J. Weber ◽  
Sebastiaan Haemers ◽  
Johannes Tramper ◽  
Arjen Rinzema

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Romana Tabassum ◽  
Shazia Khaliq ◽  
Muhammad Ibrahim Rajoka ◽  
Foster Agblevor

The thermodynamic and kinetic properties of solids state raw starch digesting alpha amylase from newly isolated Bacillus licheniformis RT7PE1 strain were studied. The kinetic values Qp, Yp/s, Yp/X, and qp were proved to be best with 15% wheat bran. The molecular weight of purified enzyme was 112 kDa. The apparent Km and Vmax values for starch were 3.4 mg mL−1 and 19.5 IU mg−1 protein, respectively. The optimum temperature and pH for α-amylase were 55°C, 9.8. The half-life of enzyme at 95°C was 17h. The activation and denaturation activation energies were 45.2 and 41.2 kJ mol−1, respectively. Both enthalpies (ΔH∗) and entropies of activation (ΔS∗) for denaturation of α-amylase were lower than those reported for other thermostable α-amylases.


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