The production of ?-amylase in batch and chemostat culture by Bacillus stearothermophilus

Davis, Paula K.; Cohen, Dan; Whitaker, Allan

doi:10.1007/bf00421985

Cited by 23 publications

(12 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Further, there was no significant variations in the enzyme yield among organic nitrogen sources (e.g., beef extract, peptone, yeast extract) incorporated at 1% level in the basal medium. Similar results were reported for B. thermooleovorans (Malhotra et al, 2000), B. stearothermophilus (Davies et al, 1980) and B. amyloliquefaciens (Babu and Satyanarayana, 1993).…”

Section: Discussionsupporting

confidence: 92%

Extracellular α-Amylase Production byBacillus brevisMTCC 7521

et al. 2008

View full text Add to dashboard Cite

Alpha amylases have various applications in food processing industries, for example, baking, brewing and distillery industries. Studies of the Ca 2+ independent α-amylase production were carried out by a strain of Bacillus brevis MTCC 7521 isolated from a brick kiln soil. The optimum temperature, pH and incubation period for amylase production were 50°C, 6.0 and 36 h, respectively. The enzyme secretion was at par in the presence of any of the carbon sources (soluble starch, cassava starch and cassava flour). B. brevis produced more amylase in presence of beef extract as nitrogen source in comparison to other organic nitrogen sources (peptone, yeast extract and casein) and asparagine, potassium nitrate, ammonium sulphate, ammonium nitrate and urea reduced the enzyme activity. The addition of Ca 2+ (10-40 mM) or surfactants (Tween 20, Tween 40, Tween 60, Tween 80, and sodium lauryl sulphate at 0.02% concentration) in culture medium did not result in further improvement in the enzyme production. The purified enzyme had a molecular mass of 205 kDa in native SDS-PAGE.

show abstract

Section: Discussionsupporting

confidence: 92%

Extracellular α-Amylase Production byBacillus brevisMTCC 7521

et al. 2008

View full text Add to dashboard Cite

show abstract

“…The negative correlation observed between amylase production and optical density (OD 560 ) supported this observation (Table 1). On the other hand, correlation between amylase production and bacterial biomass from Bradyrhizobium strain was significantly positive, confirming several authors who also found this type of linear correlation in Bacillus stearothermophilus (Davis et al, 1980), B. amyloliquefaciens (Castro et al, 1993), Nocardiopsis sp. (Stamford et al, 2001), Bacillus sp.…”

Section: Correlations Among the Parameters Evaluatedsupporting

confidence: 85%

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Oliveira

Andrade

2010

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

“…Nevertheless, the kinetic pattern of enzyme formation on yeast glycogen was fairly consistent with that of several high-producing bacterial strains such as B. subtilis (Pazlarova et al 1984), B. stearothermophilus (Welker and Campbell 1963;Davis et al 1980;Srivastava and Mathur 1984) or B. licheniformis (Meets 1972;Saito and Yamamoto 1975) when cultivated on soluble starch. can be considerd a rather common feature with regards the ecological origin of the organism as well as the amount of extracellular enzyme formed.…”

Section: Discussionsupporting

confidence: 72%

Enzyme formation by a yeast cell wall lytic Arthrobacter species: formation of amylase

John¹,

Hampel²

1992

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

The kinetics of amylolytic enzyme formation by a yeast cell wall lytic Arthrobacter species were studied. Cultivation on autoclaved cells of baker's yeast showed that amylase formation was closely related to trehalose and glycogen dissimilation. Growth on yeast glycogen (0.507o) proceeded quite rapidly (~t = 0.31 h -l ) with extensive amylase formation during exponential cell multiplication and a further low increase in activity during the stationary phase. Beside amylolytic activity [450 units (U) 1-1] the formation of a relatively high level of c~-glucosidase (90 U 1 -1) was detected, the latter almost exclusively bound to bacterial cells. Growth on 0.5°70 trehalose occurred at a reduced rate (~t = 0.22 h -1) with post-logarithmic enzyme synthesis in the stationary phase. Amylase activity attained a level of 1200 U 1-1, whereas c~-glucosidase was very low at 7.7 U 1-1. Continuous culture experiments in the chemostat showed maximal volumetric productivity of amylase (105 U1-1 h -1) at a dilution rate of 0.15h -1. Growth on various carbohydrates revealed low levels of amylolytic activity (< 100U l-I), which were increased by c~-l,4glucans and oligosaccharides such as starch, dextrin, maltotriose and maltose. On 0.5°70 maltose, growth-associated enzyme synthesis (230 U l-l) was detected at a reduced growth rate (~t = 0.14 h -1). Amylolytic enzyme preparations from the culture fluid showed an unusual cleavage pattern; acting on starch, the polymer was almost completely hydrolysed to maltotriose and maltose in a molar ratio of 3 : 1.

show abstract

The production of ?-amylase in batch and chemostat culture by Bacillus stearothermophilus

Cited by 23 publications

References 15 publications

Extracellular α-Amylase Production byBacillus brevisMTCC 7521

Extracellular α-Amylase Production byBacillus brevisMTCC 7521

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Enzyme formation by a yeast cell wall lytic Arthrobacter species: formation of amylase

Contact Info

Product

Resources

About