Molecular Cloning and Determination of the Nucleotide Sequence of Raw Starch Digesting α-Amylase from Aspergillus awamori KT-11

Matsubara, Takayoshi; Ammar, Youssef Ben; Anindyawati, Trisanti; Yamamoto, Satoru; K, Ito; Iizuka, Masaru; Minamiura, Noshi

doi:10.5483/bmbrep.2004.37.4.429

Cited by 9 publications

(3 citation statements)

References 25 publications

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“…The residues involved in the above-mentioned experimentally identified SBSs were checked for their correspondences within the particular subfamilies ( Figure S1 ), especially if they are replaced by non-aromatic residues. Thus, in the subfamily GH13_1, both SBS residues Tyr382 and Trp385 of the α-amylase from Aspergillus niger [ 49 ] were found as conserved in counterpart α-amylases from ( Table 2 ) Aspergillus awamori ([ 64 ]; GenBank: BAD06002.1), Aspergillus flavus ([ 65 ]; AAF14264.1), Aspergillus kawachii ([ 66 ]; BAD01051.1), Aspergillus oryzae ([ 67 ]; CAA31218.1), Aspergillus shirousami ([ 68 ]; BAA01255.1), Fusicoccum sp. BCC4124 ([ 69 ]; ABG48762.1), Lipomyces spencermartinsiae ([ 70 ]; AAC49622.1) and Lipomyces starkeyi ([ 71 ]; AAN75021.1).…”

Section: Resultsmentioning

confidence: 99%

In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites

Janíčková

Janeček

2021

Molecules

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This study brings a detailed bioinformatics analysis of fungal and chloride-dependent α-amylases from the family GH13. Overall, 268 α-amylase sequences were retrieved from subfamilies GH13_1 (39 sequences), GH13_5 (35 sequences), GH13_15 (28 sequences), GH13_24 (23 sequences), GH13_32 (140 sequences) and GH13_42 (3 sequences). Eight conserved sequence regions (CSRs) characteristic for the family GH13 were identified in all sequences and respective sequence logos were analysed in an effort to identify unique sequence features of each subfamily. The main emphasis was given on the subfamily GH13_32 since it contains both fungal α-amylases and their bacterial chloride-activated counterparts. In addition to in silico analysis focused on eventual ability to bind the chloride anion, the property typical mainly for animal α-amylases from subfamilies GH13_15 and GH13_24, attention has been paid also to the potential presence of the so-called secondary surface-binding sites (SBSs) identified in complexed crystal structures of some particular α-amylases from the studied subfamilies. As template enzymes with already experimentally determined SBSs, the α-amylases from Aspergillus niger (GH13_1), Bacillus halmapalus, Bacillus paralicheniformis and Halothermothrix orenii (all from GH13_5) and Homo sapiens (saliva; GH13_24) were used. Evolutionary relationships between GH13 fungal and chloride-dependent α-amylases were demonstrated by two evolutionary trees—one based on the alignment of the segment of sequences spanning almost the entire catalytic TIM-barrel domain and the other one based on the alignment of eight extracted CSRs. Although both trees demonstrated similar results in terms of a closer evolutionary relatedness of subfamilies GH13_1 with GH13_42 including in a wider sense also the subfamily GH13_5 as well as for subfamilies GH13_32, GH13_15 and GH13_24, some subtle differences in clustering of particular α-amylases may nevertheless be observed.

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Section: Resultsmentioning

confidence: 99%

In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites

Janíčková

Janeček

2021

Molecules

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“…It would be of value to reduce the cost of gelatinization and simplify the process of starch conversion. It has so far been reported that fungi and yeast (Matsubara et al, 2004;Ramachandran et al, 2008) were good producers of raw starch digesting amylases, while there were few reports on raw starch degradation by Bacillus sp. -amylases.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterization of an α-amylase with raw starch digestibility fromBacillus sp. YX-1

Liu

2009

Ann. Microbiol.

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The complete gene (amy) that encoding a raw starch digesting -amylase (BYXA) from Bacillus sp. YX-1 was cloned, sequenced and expressed in Escherichia coli. The amy gene consisted of 1545 base pairs and encoded a protein of 514 amino acid residues with a calculated molecular mass of 58 kDa. The recombinant protein was purified by Ni 2+ affinity chromatography and subsequently characterized. The optimal pH and temperature for the purified recombinant enzyme were 5.5 and 45 °C, respectively. The enzyme showed stability over a pH range of 5.0-11.0 and below 50 °C. The enzyme exhibited remarkable digestibility towards raw starch at low pH values, which was valuable in starch processing industry.

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“…This process, although currently used by starch processing industries, is energy intensive thus increasing the production cost of starch-based products. With the view of reducing the energy cost, a worldwide interest has been focused on raw starch degrading enzymes (RSDE) in recent years [3][4][5][6]. Microorganisms reported to be good producers of RSDE include Aspergillus sp.…”

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confidence: 99%

Improved Production of Raw Starch Degrading Enzyme by Aspergillus oryzae F-30 Using Methyl Glucoside Sesqui-Stearate

Sun

Wang

Jian-wen³

et al. 2008

Appl Biochem Biotechnol

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The effect of methyl glucoside sesqui-stearate (MGS) on the production of raw starch degrading enzyme (RSDE) by Aspergillus oryzae F-30 was studied in this paper. The activity of RSDE formed by Aspergillus oryzae F-30 was enhanced dramatically by the addition of MGS to the medium. As a result, with the addition of 1.5 g MGS in 1 L basal medium, RSDE activity and productivity were 107 U mL(-1) and 1.49 U mL(-1) h(-1), 4.3-fold and 7.1-fold greater than the values obtained in the basal medium, respectively. The effect of MGS on the synthesis of RSDE by Aspergillus oryzae F-30 was also studied on a molecular level. It was observed that the regulation of RSDE synthesis in Aspergillus oryzae F-30 occurs at both transcriptional and translational level and the enzyme synthesis was provoked by the addition of MGS at transcriptional level.

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Molecular Cloning and Determination of the Nucleotide Sequence of Raw Starch Digesting α-Amylase from Aspergillus awamori KT-11

Cited by 9 publications

References 25 publications

In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites

In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites

Molecular cloning and characterization of an α-amylase with raw starch digestibility fromBacillus sp. YX-1

Improved Production of Raw Starch Degrading Enzyme by Aspergillus oryzae F-30 Using Methyl Glucoside Sesqui-Stearate

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