Enzymic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli

Lo, Huei-Fen; Lin, Long-Liu; Chen, Hsiang-Ling; Hsu, Wen-Hwei; Chang, Chung‐Ju

doi:10.1016/s0032-9592(00)00273-9

Cited by 46 publications

(22 citation statements)

References 46 publications

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“…A stimulatory effect of SDS (6%) on amylase activity and stability in Bacillus sp. strain TS-23 was documented by Lo et al (2001). From the previous reports and the present study, it was evident that the same surfactant could have different effect on the activity of the same enzyme in the same microorganism, or on the activity of different enzymes in the same microorganism, as previously discussed by Reddy et al (1999).…”

Section: Effect Of Surfactants On Amylase Activitysupporting

confidence: 78%

“…strain KSM-K38 (Hagihara et al, 2001). These results suggested that the effect of Hg 2+ could vary among the microbial amylases, as observed for other heavy metal ions such as Cd 2+ , Co 2+ , Fe 2+ and Ni 2+ (Pandey et al, 2000;Lo et al, 2001;Dey et al, 2003). In addition, the presence of 5 mM Zn 2+ had a slight stimulatory effect on amylase activity ( (1 mM) showed a slight inhibitory effect on enzyme activity.…”

Section: +mentioning

confidence: 64%

“…The importance of cysteine residues for catalysis was previously described for amylases independently of their origin (Pandey et al, 2000;Lo et al, 2001;Díaz et al, 2003). From the results, it could concluded that the broad range of pH activity and stability profiles, optimum activity at lower pH and the high tolerance towards surfactants such as SDS, Triton X-100 and Tween-80 could make these rhizobial amylases attractive for both basic research and industrial biotechnological processes.…”

Section: Effect Of Inhibitors On Amylase Activitymentioning

confidence: 73%

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Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Oliveira

Andrade

2010

Braz. arch. biol. technol.

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Section: Effect Of Surfactants On Amylase Activitysupporting

confidence: 78%

Section: +mentioning

confidence: 64%

Section: Effect Of Inhibitors On Amylase Activitymentioning

confidence: 73%

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Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Oliveira

Andrade

2010

Braz. arch. biol. technol.

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“…The effect of metal ions and some chemicals, including chelating agents and inhibitors on amylolytic activity, was studied by pre-incubating the enzyme in the presence of substances with a final concentration of 3 or 5 mM for 30 min at 50ºC, and then performing the assay in the presence of the same substances at the optimum temperature (11,26). All metals used were in the chloride form.…”

Section: Effect Of Some Metal Ions and Chemical Agents On Enzyme Actimentioning

confidence: 99%

Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

Aygan¹,

Arikan²,

Korkmaz³

et al. 2008

Braz. J. Microbiol.

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An alkaliphilic and highly thermostable α-amylase producing Bacillus sp. was isolated from Van soda lake. Enzyme synthesis occurred at temperatures between 25ºC and 40ºC. Analysis of the enzyme by SDS-PAGE revealed a single band which was estimated to be 66 kDa. The enzyme was active in a broad temperature range, between 20ºC and 90ºC, with an optimum at 50ºC; and maximum activity was at pH 10.5. The enzyme was almost completely stable up to 80ºC with a remaining activity over 90% after 30 min pre-incubation. Thermostability was not increased in the presence of Ca2+ . An average of 75% and 60ºC of remaining activity was observed when the enzyme was incubated between pH 5 and 9 for 1 h and for 2 h, respectively. The activity of the enzyme was inhibited by SDS and EDTA by 38% and 34%, respectively.

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“…Biotechnological interest in microbial amylases has increased recently [6,8,9,11,20,21]. Amylases produced by thermophilic and thermotolerant microorganisms are especially interesting because they are usually thermostable, and can be used in saccharification processes that occur at high temperatures [2,3,4,5,15,20].…”

Section: Introductionmentioning

confidence: 99%

Rhizopus microsporus var. rhizopodiformis : a thermotolerant fungus with potential for production of thermostable amylases

Peixoto

Jorge

Terenzi

et al. 2003

International Microbiology

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The effect of several nutritional and environmental parameters on growth and amylase production from Rhizopus microsporus var. rhizopodiformis was analysed. This fungus was isolated from soil of the Brazilian "cerrado" and produced high levels of amylolytic activity at 45 degrees C in liquid medium supplemented with starch, sugar cane bagasse, oat meal or cassava flour. Glucose in the culture medium drastically repressed the amylolytic activity. The products of hydrolysis were analysed by thin layer chromatography, and glucose was detected as the main component. The amylolytic activity hydrolysed several substrates, such as amylopectin, amylase, glycogen, pullulan, starch, and maltose. Glucose was always the main end product detected by high-pressure liquid chromatography analysis. These results indicated that the amylolytic activity studied is a glucoamylase, but there were also low levels of alpha-amylase. As compared to other fungi, R. microsporus var. rhizopodiformis can be considered an efficient producer of thermostable amylases, using raw residues of low cost as substrates. This information is of technological value, considering the importance of amylases for industrial hydrolysis.

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Enzymic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli

Cited by 46 publications

References 46 publications

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

Rhizopus microsporus var. rhizopodiformis : a thermotolerant fungus with potential for production of thermostable amylases

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