Mechanisms of action of the ?-amylase of Micromonospora melanosporea

Kelly, Catherine T.; Collins, Bernadette S.; Fogarty, William N.; Doyle, Evelyn

doi:10.1007/bf00205059

Cited by 12 publications

(3 citation statements)

References 15 publications

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“…The same applies to CaCl 2 , 0.12 g/l [25], 1 g/l [26]. A similar observation is made for salts concentration: FeSO 4 (0.1 g/l) [27], MnSO 4 (0.1 g/l) [27] or 0.4 g/l [21], MgCl 2 (0.2 g/l) [28]. These differences are explained by the diversity of the medium constitution used for each case and also by the corresponding micro-organism.…”

Section: The Evaluation Of the X 0 Stationary Pointsupporting

confidence: 73%

An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder

Scheherazed

Bennamoun

Amel

et al. 2016

ABB

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In this work, sequential optimization strategy, based on statistical designs, was employed to enhance the production of α-amylase by Aspergillus niger ATCC 16404. This statistical study consists of optimizing the factors that influence the production of α-amylase of A. niger ATCC 16404. Indeed, another statistical study has allowed the selection of 5 factors (pH, starch, yeast extract, "corn steep liquor", CaCl2 and salts) affecting both the development of mould (biomass) and that of the enzyme production. The central composite design allows the determination of the optimum of these selected factors and a quadratic model explains the factor reaction. Thus, the "ridge analysis" method, has led to maximizing the experimental reaction. The results indicate that the production rate of α-amylase is maximized in the presence of starch at 8.97 g/l, yeast extract at 2.86 g/l, CaCl2 at 1.224 g/l, salts (composed of 25% FeSO4, 7H2O, 25% MnSO4 and 50% MgCl2, 6H2O): FeSO4, 7H2O, MnSO4 0.1518 g/l and MgCl2, 6H2O at 0.3036 g/l. As for the pH, it is maintained at the rate of 5.68.

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Section: The Evaluation Of the X 0 Stationary Pointsupporting

confidence: 73%

An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder

Scheherazed

Bennamoun

Amel

et al. 2016

ABB

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“…A number of maltogenic α-amylases from actinomycetes [28,[30][31][32] have been reported to form high levels of maltose, ranging from 53% to greater than 80% (w/w). However, the only reported fungal α-amylase capable of producing exceptionally high levels of maltose (74%, w/w) from starch was by a strain of P. expansum [27].…”

Section: ±2mentioning

confidence: 99%

Gene Cloning, Heterologous Expression, and Characterization of a High Maltose-Producing α-Amylase of Rhizopus oryzae

Song

Zuo

Niu

et al. 2011

Appl Biochem Biotechnol

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A putative α-amylase gene, designated as RoAmy, was cloned from Rhizopus oryzae. The deduced amino acid sequence showed the highest (42.8%) similarity to the α-amylase from Trichoderma viride. The RoAmy gene was successfully expressed in Pichia pastoris GS115 under the induction of methanol. The molecular weight of the purified RoAmy determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis was approximately 48 kDa. The optimal pH and temperature were 4-6 and 60 °C, respectively. The enzyme was stable at pH ranges of 4.5-6.5 and temperatures below 50 °C. Purified RoAmy had a K(m) and V(max) of 0.27 mg/ml and 0.068 mg/min, respectively, with a specific activity of 1,123 U/mg on soluble starch. Amylase activity was strongly inhibited by 5 mM Cu(2+) and 5 mM Fe(2+), whereas 5 mM Ca(2+) showed no significant effect. The RoAmy hydrolytic activity was the highest on wheat starch but showed only 55% activity on amylopectin relative to soluble corn starch, while the pullulanase activity was negligible. The main end products of the polysaccharides tested were glucose and maltose. Maltose reached a concentration of 74% (w/w) with potato starch as the substrate. The enzyme had an extremely high affinity (K(m) = 0.22 mM) to maltotriose. A high ratio of glucose/maltose of 1:4 was obtained when maltotriose was used at an initial concentration of 40 mM.

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“…strain ST04 (15). The mechanisms to produce high levels of maltose were postulated to involve these ␣-amylases exhibiting significant multimolecular reactions, including condensation and transglycosylation, in addition to their hydrolytic activity (14,(16)(17)(18) or exhibiting an exo-type maltose-forming ␣-amylase action pattern (13,15). Saccharifying ␣-amylases, mainly ␣-amylase from Aspergillus oryzae, are used in the industrial production of maltose syrups with a 40 to 50% maltose content (19).…”

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confidence: 99%

Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

Zhou

Zhang

et al. 2018

Appl Environ Microbiol

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The gene encoding the novel amylolytic enzyme designated CoMA was cloned from sp. strain EGB. The deduced amino acid sequence contained a predicted lipoprotein signal peptide (residues 1 to 18) and a conserved glycoside hydrolase family 13 (GH13) module. The amino acid sequence of CoMA exhibits low sequence identity (10 to 19%) with cyclodextrin-hydrolyzing enzymes (GH13_20) and is assigned to GH13_36. The most outstanding feature of CoMA is its ability to catalyze the conversion of maltooligosaccharides (≥G3) and soluble starch to maltose as the sole hydrolysate. Moreover, it can hydrolyze γ-cyclodextrin and starch to maltose and hydrolyze pullulan exclusively to panose with relative activities of 0.2, 1, and 0.14, respectively. CoMA showed both hydrolysis and transglycosylation activities toward α-1,4-glycosidic bonds but not to α-1,6-linkages. Moreover, glucosyl transfer was postulated to be the major transglycosidation reaction for producing a high level of maltose without the attendant production of glucose. These results indicated that CoMA possesses some unusual properties that distinguish it from maltogenic amylases and typical α-amylases. Its physicochemical properties suggested that it has potential for commercial development. The α-amylase from sp. EGB, which was classified to the GH13_36 subfamily, can catalyze the conversion of maltooligosaccharides (≥G3) and soluble starch to maltose as the sole hydrolysate. An action mechanism for producing a high level of maltose without the attendant production of glucose has been proposed. Moreover, it also can hydrolyze γ-cyclodextrin and pullulan. Its biochemical characterization suggested that CoMA may be involved the accumulation of maltose in media.

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Mechanisms of action of the ?-amylase of Micromonospora melanosporea

Cited by 12 publications

References 15 publications

An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder

An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder

Gene Cloning, Heterologous Expression, and Characterization of a High Maltose-Producing α-Amylase of Rhizopus oryzae

Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

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Mechanisms of action of the ?-amylase of Micromonospora melanosporea

Cited by 12 publications

References 15 publications

An Optimization Study of α-Amylase Production by &lt;i&gt;Aspergillus niger&lt;/i&gt; ATCC 16404 Grown on Orange Waste Powder

An Optimization Study of α-Amylase Production by &lt;i&gt;Aspergillus niger&lt;/i&gt; ATCC 16404 Grown on Orange Waste Powder

Gene Cloning, Heterologous Expression, and Characterization of a High Maltose-Producing α-Amylase of Rhizopus oryzae

Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

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An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder

An Optimization Study of α-Amylase Production by <i>Aspergillus niger</i> ATCC 16404 Grown on Orange Waste Powder