Thermal adaptation of α-amylases: a review

Hiteshi, Kalpana; Gupta, Reena

doi:10.1007/s00792-014-0674-5

Cited by 32 publications

(19 citation statements)

References 69 publications

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“…However, the enzyme activity was enhanced with the presence of Ca 2+ , which is in agreement with previous reports by Li et al and Mohammad et al . Previous reports have shown that most amylases are dependent on Ca 2+ for their structural integrity and stability . In contrast, some Ca 2+ independent amylases had also been reported .…”

Section: Resultssupporting

confidence: 92%

“…A). However, Bekler and Güven reported an optimum temperature of 60°C for an amylase from Anoxybacillus KP1 from the Diyadin Hot Springs in Turkey. Kikani and Singh observed that an isolated amylase from Bacillus amyloliquifaciens TSWK1‐1 from the Tulsi Shyam Hot Springs in India was optimally active at 70°C.…”

Section: Resultsmentioning

confidence: 99%

“…Among the extremophiles, thermophilic microorganisms are of special interest as enzymes produced by these organisms generally show maximal activity and stability at high temperatures . The advantages of thermostable amylases in industrial processes are, for instance, reduction in cooling costs, increase in substrate solubility, reduced risk of microbial contamination, and resistance to denaturing agents and proteolytic enzymes . We have previously reported the identification of a thermophilic bacterium Anoxybacillus sp.…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of a novel and versatile α-amylase from thermophilicAnoxybacillussp. YIM 342

et al. 2015

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An extracellular thermophilic a-amylase (1, 4-a-D-glucanohydrolase, EC 3.2.1.l) from Anoxybacillus sp. YIM 342 was partially purified by ultrafiltration followed by ammonium sulfate fractionation and dialysis. This procedure was followed by a single purification step using gel filtration chromatography to give a 10.41% yield, 1912.2 U/mg specific activity, and 32-fold purification enrichment. The molecular mass of the purified a-amylase was determined to be 68 kDa using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum temperature and pH of the a-amylase activity were 80°C and 9.0, respectively. Furthermore, the high hydrolysis rate toward amylose and amylopectin suggested the enzyme has significant potential for applications in starch degradation. The K m and V max of the amylase toward soluble starch was 4.18 mg/mL and 7.48 mmol/min/mg, respectively. This enzyme hydrolyzes soluble starch to glucose, maltose, and maltotriose, indicating that the amylase represents a promising candidate for applications in the biofuel industry.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of a novel and versatile α-amylase from thermophilicAnoxybacillussp. YIM 342

et al. 2015

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“…The solubility of some proteins will increase at low salt concentrations (salting in), but precipitate with the increase of the concentrations (salting out). Salt concentrations threshold for salting-in or salting out differ amongst proteins, depending on the type and the amount of amino acids on the protein surface (Hiteshi and Gupta, 2014). This explains why, despite having the highest activity, Fraction 2 has a lower specific activity compared to Fraction 3.…”

Section: Ammonium Sulfat Precipitationmentioning

confidence: 99%

Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

2018

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Bio-based industries require stable enzymes in a broad range of environmental conditions. Extremophiles have attracted more interests as the source of such enzymes, one of which is α-amylase. This study aimed to purify and characterize α-amylase produced by a thermo-halophilic bacterium PLS 75 isolated from underwater fumaroles. Ammonium sulfate precipitation results showed that the highest specific α-amylase activity (21.7 U/mg) obtained at 40-60% saturation level, with a purity of 7.7-fold of the crude extract with 16.2% yield. Further purification using DEAE Sepharose column chromatography increased the enzyme purity 11.1-fold of the crude extract with 7.1% yield. Specific activity after column chromatography purification was 31.3 U/mg. The pure enzyme had a low molecular weight of 14 kDa. The enzyme showed the highest activity at 80 °C and pH 5. The activity increased to 126% when in methanol, while decreased when in ethyl acetate and chloroform. The characteristics of α-amylase with low molecular weight, which was active in acidic condition, stable in polar and non-polar solvents, may be used for for specific industrial needs.

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“…Cold-adapted enzymes that catalyze the reaction at low temperatures but lose activities by a moderate heating are highly beneficial to industries and biotechnology and have obtained increasing attentions in recent years [ 15 – 18 ]. For example, cold-adapted α -amylases can be added to detergents for cold washing to save the energy, reduce the wear, and protect the color of fabrics [ 19 – 21 ]. In baking processes, they can be used to shorten the dough fermentation time, quickly terminate the reaction of other enzymes, and improve the properties of the bread [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Characterization of a Novelα-Amylase from Antarctic Sea Ice BacteriumPseudoalteromonassp. M175 and Its Primary Application in Detergent

Wang

Kan

Ren

et al. 2018

BioMed Research International

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A novel cold-adapted and salt-tolerant α-amylase gene (amy175) from Antarctic sea ice bacterium Pseudoalteromonas sp. M175 was successfully cloned and expressed. The open reading frame (ORF) of amy175 had 1722 bp encoding a protein of 573 amino acids residues. Multiple alignments indicated Amy175 had seven highly conserved sequences and the putative catalytic triad (Asp244, Glu286, and Asp372). It was the first identified member of GH13_36 subfamily which contained QPDLN in the CSR V. The recombinant enzyme (Amy175) was purified to homogeneity with a molecular mass of about 62 kDa on SDS-PAGE. It had a mixed enzyme specificity of α-amylase and α-glucosidase. Amy175 displayed highest activity at pH 8.0 and 25°C and exhibited extreme salt-resistance with the maximum activity at 1 M NaCl. Amy175 was strongly stimulated by Mg2+, Ni2+, K+, 1 mM Ca2+, 1 mM Ba2+, 1 mM Pb2+, 1 mM sodium dodecyl sulphate (SDS), and 10% dimethyl sulfoxide (DMSO) but was significantly inhibited by Cu2+, Mn2+, Hg2+, 10 mM β-mercaptoethanol (β-ME), and 10% Tween 80. Amy175 demonstrated excellent resistance towards all the tested commercial detergents, and wash performance analysis displayed that the addition of Amy175 improved the stain removal efficiency. This study demonstrated that Amy175 would be proposed as a novel α-amylase source for industrial application in the future.

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Thermal adaptation of α-amylases: a review

Cited by 32 publications

References 69 publications

Purification and characterization of a novel and versatile α-amylase from thermophilicAnoxybacillussp. YIM 342

Purification and characterization of a novel and versatile α-amylase from thermophilicAnoxybacillussp. YIM 342

Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

Molecular Cloning and Characterization of a Novelα-Amylase from Antarctic Sea Ice BacteriumPseudoalteromonassp. M175 and Its Primary Application in Detergent

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