Substrate preference of a Geobacillus maltogenic amylase: A kinetic and thermodynamic analysis

Nasrollahi, Samira; Golalizadeh, Leila; Sajedi, Reza H.; Taghdir, Majid; Asghari, S. Mohsen; Rassa, Mehdi

doi:10.1016/j.ijbiomac.2013.04.063

Cited by 12 publications

(6 citation statements)

References 43 publications

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“…G3Amy inefficiently hydrolyzed cyclodextrins (Table 2) as compared to that of other exo-α-amylases such as Geobacillus maltogenic amylases (Mehta and Satyanarayana 2013;Nasrollahi et al 2013). This indicated that the nonreducing end of a substrate was helpful to recognize the substrate, but not essential for hydrolysis by G3Amy unlike β-amylases.…”

Section: Discussionmentioning

confidence: 96%

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

Kamon

Sumitani

Tani

et al. 2015

Appl Microbiol Biotechnol

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A maltotriose-forming amylase (G3Amy) from Kitasatospora sp. MK-1785 was successfully isolated from a soil sample by inhibiting typical extracellular α-amylases using a proteinaceous α-amylase inhibitor. G3Amy was purified from the MK-1785 culture supernatant and characterized. G3Amy produced maltotriose as the principal product from starch and was categorized as an exo-α-amylase. G3Amy could also transfer maltotriose to phenolic and alcoholic compounds. Therefore, G3Amy can be useful for not only maltotriose manufacture but also maltooligosaccharide-glycoside synthesis. Further, the G3Amy gene was cloned and expressed in Escherichia coli cells. Analysis of its deduced amino acid sequence revealed that G3Amy consisted of an N-terminal GH13 catalytic domain and two C-terminal repeat starch-binding domains belonging to CBM20. It is suggested that natural G3Amy was subjected to proteolysis at N-terminal region of the anterior CBM20 in the C-terminal region. As with natural G3Amy, recombinant G3Amy could produce and transfer maltotriose from starch.

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Section: Discussionmentioning

confidence: 96%

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

Kamon

Sumitani

Tani

et al. 2015

Appl Microbiol Biotechnol

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“…IM6501 (WP021322528.1), 68.66% with neopullulanase (NPase) of Geobacillus strearothermophilus (AAK15003.1), and 69.35% with MAase of Geobacillus spp. (ADM86931.1) . The analysis of amino acid sequence showed that CDase‐ZNU has four conserved regions which are the common conserved regions in the CD‐hydrolyzing enzymes and they include CDase, NPase, and MAase.…”

Section: Resultsmentioning

confidence: 99%

“…From thermostability point of view, the incubation conditions caused CDase‐ZNU to retain a high value (70%) of its activity at 65 °C for 60 min, while it was 50 °C for 30 min in CDase from Paenibacillus spp . and 60 °C for 60 min in MAase from Geobacillus spp …”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that the CDs specificity of recombinant CDase isolated from E. faecium K‐1 was about 96 times higher as compared to starch in which non‐significant hydrolysis was observed with polysaccharides including starch and glycogen. The idea was that the α‐1,6 glycosidic linkage could not be attacked by the enzyme . Therefore, the substrate specificity of CDase‐ZNU for branched substrates is less than that for CDs.…”

Section: Discussionmentioning

confidence: 99%

“…IM6501 (WP021322528.1), NPase in G. strearothermophilus (AAK15003.1) and MAase in Geobacillus spp. (ADM86931.1) . These residues include Asp 328 , Glu 357 , and Asp 424 which are conserved in all α‐amylase families.…”

Section: Discussionmentioning

confidence: 99%

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Genetic and Biochemical Characterization of a Novel Thermostable Cyclomaltodextrinase From Anoxybacillus flavithermus

et al. 2018

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A strain of thermophilic Anoxybacillus flavithermus is characterized bacteriologically and biochemically. Then, the gene responsible for encoding cyclomaltodextrinase (CDase) in this bacterium is isolated, cloned, and overexpressed. The sequence of the CDase is recorded in GenBank with accession number KT633577.1. Biochemical and structural characterization of the enzyme shows that CDase with molecular weight of 72 kDa is active in the optimum temperature and pH of 65 °C and 7.0, respectively and it exists in oligomeric forms. It is observed that α‐cyclodextrin (α‐CD) has higher kcat/km value as compared to starch, glycogen, β‐ and γ‐CD and is therefore a more specific substrate for the enzyme. Also, the addition of metal ions such as K1+ and Na1+ can help to improve the catalytic activity, while Fe2+ and Cu+2 have inhibitory effects on the activity of the enzyme. It is also found that the catalytic activity of the enzyme increases in the presence of 5 mM β‐mercaptoethanol, EDTA, DTT, and PMSF. Thin layer chromatography (TLC) shows that glucose and maltose are the main products of CDase‐catalyzed reaction of α‐, β‐, and γ‐CD hydrolysis. Considering the modeling results, the CDase consists of three domains in which the central domain is the catalytic core containing active site residues. Based on its specificity for various substrates, the new homologue of CDase can be considered as a suitable candidate for industrial applications involving production of maltose and glucose from α‐, β‐, and γ‐CD or a mixture of these compounds in extreme conditions of temperature.

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Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis: structural and functional analyses

et al. 2021

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Substrate preference of a Geobacillus maltogenic amylase: A kinetic and thermodynamic analysis

Cited by 12 publications

References 43 publications

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

Genetic and Biochemical Characterization of a Novel Thermostable Cyclomaltodextrinase From Anoxybacillus flavithermus

Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis: structural and functional analyses

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