Thermophilic archaeal amylolytic enzymes

Lévêque, Emmanuel; Janeček, Štefan; Haye, Bernard; Belarbi, A.

doi:10.1016/s0141-0229(99)00142-8

Cited by 185 publications

(106 citation statements)

References 55 publications

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“…Najafi et al (2005) observed that the α-amylase from Bacillus subtilis AX20 did not have an obligate requirement for divalent metal ions to be active and its activity was not stimulated in the presence of metal ions. A stronger inhibitory effect was observed in the presence of Cu , Cu 2+ and Ba 2+ ions could be due to competition between the exogenous cations and the protein-associated cation, resulting in decreased metalloenzyme activity (15).…”

Section: Effect Of Metal Ionsmentioning

confidence: 98%

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Properties of an amylase from thermophilic Bacillus SP.

Carvalho

Corrêa

Silva

et al. 2008

Braz. J. Microbiol.

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α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90ºC. The enzyme was stable for 1 h at temperatures ranging from 40-50ºC while at 90ºC, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90ºC for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. . In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45ºC. The amylase exhibited more than 70% activity when incubated for 1 h at 50ºC with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50ºC in the presence of the detergent brands Omo ® , Campeiro ® and Tide ® , respectively.

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Section: Effect Of Metal Ionsmentioning

confidence: 98%

“…Thermostable α-amylases have extensive commercial applications in starch processing, brewing and sugar production, desizing in textile industries and in detergent manufacturing processes (10,15).…”

Section: Introductionmentioning

confidence: 99%

Properties of an amylase from thermophilic Bacillus SP.

Carvalho

Corrêa

Silva

et al. 2008

Braz. J. Microbiol.

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“…The inhibition of α-amylase by Hg 2+ might indicate the importance of the enzyme function [10]. The inhibition of enzyme activity by metallic ions could be due to competition between the exogenous cations and the protein-associated cations, resulting in decreased metalloenzyme activity [38]. Oboh and Ajele [39] and Mohapatra et al [40] in their previous studies have reported metallic chlorides as most potent activators of amylase.…”

Section: Characterization Of α-Amylasementioning

confidence: 99%

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

David¹,

Femi²,

Gbenga³

et al. 2017

J Bioremediat Biodegrad

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This study was designed to purify and characterize of α-amylase from pure strain of Bacillus subtilis. The crude α-amylase was purified by ammonium sulphate precipitation, then loaded on DEAE Sephadex A-50 ion exchange chromatography and gel filtration. The effect of pH, temperature and metal ions were investigated on the purified enzyme. The single protein band on SDS-PAGE suggested that the enzyme was homogenous. Two different activity peaks were observed in ion exchange chromatography designated pool A and pool B with the 8% and 4% yield, 15.93 and 6.44 purification fold and specific activity 2.55 μmol/min/mg and 1.03 μmol/min/mg respectively. The two fractions revealed the same optimum pH 7.0 for the α-amylase activity while the enzyme was relatively stable at pH 4.0 and 7.0 between 20 to 40 minutes and 60 to 80 minutes for pool A and pH 8.0 between 40 and 100 minutes for pool B. At 40°C, optimum temperature was reached, and amylase activity was maintained at 75% and 70% temperature stability between 60 to 80 minutes for pool A and B, less than 20%, the residual activity at 60°C and 70°C was recorded. The incubation of α-amylase with Na + and Zn 2+ ions enhanced/activate the enzyme activity correspondingly, Al 3+ and K + ions exhibited varied degree of inhibition while Ca 2+ and Hg 2+ ions caused total inhibition on α-amylase activity. The ability of purified α-amylase from Bacillus subtilis under wide range of temperatures and pH suggests its applications in industries and bioremediation of effluent discharge on food processing sites.

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“…In the case of T. hydrothermalis amylopullulanase activity did not affect from Na + or Mg 2+ while Mn 2+ cations increase its activity. The inhibitory effect of some metal cations such as Ni 2+ and Cu 2+ has been observed for almost all amylopullulanases (Rudiger et al 1995;Dong et al 1997;Duffner et al 2000;Leveque et al 2000).…”

Section: Effects Of Metal Ions and Other Reagentsmentioning

confidence: 99%

“…Thus it seems a basic necessity to identify suitable thermoactive and thermostable pullulanase which improves saccharification rate and process yield (Saha et al 1990;Gantelet et al 1998;Duffner et al 2000;Leveque et al 2000). Pullulanase type II (amylopullulanase) hydrolyzes the α-1,4 and α-1,6 glycosidic linkages in branched substrates and α-1,4 glycosidic bonds in pullulan (Matzke et al 2000).…”

Section: Introductionmentioning

confidence: 99%

An investigation on acarbose inhibition and the number of active sites in an amylopullulanase (L14-APU) from an Iranian Bacillus sp.

et al. 2008

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An amylopullulanase (L14-APU) from an Iranian thermophilic bacterium was purified and the effect of acarbose, as a general inhibitor of α-amylases, on pullulan and starch hydrolysis catalyzed by L14-APU was investigated. The inhibition is a competitive type whereas inhibition constants for pullulan and starch are 99 µM and 72 µM, respectively. Investigation of the reaction rate in a system contains competitive substrates and the inhibition type of acarbose in presence of different substrates suggests that L14-APU possesses only one active site for two activities. The analysis of metal ions and other reagents effects has shown that Ca 2+ , Mg 2+ , Mn 2+ and Co 2+ enhanced both activities of the enzyme while N-bromosuccinimide treatment leads to the complete inactivation of the enzyme. The enzyme activity increased in the presence of low concentration of SDS as a surfactant.

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Thermophilic archaeal amylolytic enzymes

Cited by 185 publications

References 55 publications

Properties of an amylase from thermophilic Bacillus SP.

Properties of an amylase from thermophilic Bacillus SP.

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

An investigation on acarbose inhibition and the number of active sites in an amylopullulanase (L14-APU) from an Iranian Bacillus sp.

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