Identification of an acidic α-amylase from Alicyclobacillus sp. A4 and assessment of its application in the starch industry

  title={Identification of an acidic $\alpha$-amylase from Alicyclobacillus sp. A4 and assessment of its application in the starch industry},
  author={Yingguo Bai and Huo-qing Huang and Kun Meng and Pengjun Shi and Peilong Yang and Huiying Luo and Chunliang Luo and Yukun Feng and Wei Zhang and Bin Yao},
  journal={Food Chemistry},

A Novel Multifunctional α-Amylase from the Thermophilic Fungus Malbranchea cinnamomea: Biochemical Characterization and Three-Dimensional Structure

A novel α-amylase from the thermophilic fungus, Malbranchea cinnamomea was purified, characterized and crystallized in the present study and displayed the highest amino acid sequence homology with the reported α- amylases.

Purification and Characterization of α-amylase from a Novel Thermoalkalophilic Strain of Bacillus sonorensis GV2 Isolated from Mushroom Compost

The MALDI peptide mass fingerprint analysis of the reduced and carboxymethylated amylase digested with chymotrypsin indicated that this partial amino acid sequence was homologous by a score of 6 with UDP transferalyase, suggesting about the potential role of this α-amylase for raw starch degrading applications in the relevant industry.

A New α-Galactosidase from Thermoacidophilic Alicyclobacillus sp. A4 with Wide Acceptor Specificity for Transglycosylation

An α-galactosidase gene (gal36A4) of glycosyl hydrolase family 36 was identified in the genome of Alicyclobacillus sp. A4. It contains an ORF of 2,187 bp and encodes a polypeptide of 728 amino acids

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

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.

Purification and biochemical characterization of an acidophilic amylase from a newly isolated Bacillus sp. DR90

Thin layer chromatography analyses displayed that maltose and glucose are the main products of the enzyme reaction on starch, and the enzyme may be utilized as a novel candidate for industrial applications.

Characterization of purified α-amylase produced by Aspergillus terreus NCFT 4269.10 using pearl millet as substrate

Owing to its noteworthy stability in the presence of detergents, additives, inhibitors, and metal ions, this α-amylase could be an impending enzyme for significant industrial exploitations.

A novel saccharifying α‐amylase of Antarctic psychrotolerant fungi Geomyces pannorum: Gene cloning, functional expression, and characterization

The preliminary study on the high‐glucose‐producing α‐amylase with detailed enzymatic properties shows a potential application prospect in syrup industry.

Molecular Identification of a Bacillus mojavensis UMF29 Producing a Novel Raw-starch Degrading Alpha-amylase

Microbial alpha-amylases demonstrate more compatibility with industrial demands. These industrial enzymes have potential applications in various industrial parts, e.g., starch processing, brewing,



Purification, properties and structural aspects of a thermoacidophilic alpha-amylase from Alicyclobacillus acidocaldarius atcc 27009. Insight into acidostability of proteins.

It is proposed that these proteins have adapted to the acidic environment by reducing the density of both positive and negative charges at their surface, that this effect circumvents electrostatic repulsion of charged groups at low pH, and thereby contributes to the acidostability of these proteins.

A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability

A highly pH-adaptable and stable xylanase (XynA4) from the thermoacidophilic Alicyclobacillus sp.

Expression of an extremely acidic β-1,4-glucanase from thermoacidophilic Alicyclobacillus sp. A4 in Pichia pastoris is improved by truncating the gene sequence

Of the four forms of CelA4 studied, CelA 4T was produced in highest yield and had the most favorable physical properties; therefore, it has potential for use in the feed industry.

Biochemical Characterization of Raw-starch-digesting Alpha Amylase Purified from Bacillus amyloliquefaciens

The purifiedAlpha amylase of Bacillus amyloliquefaciens produced by submerged fermentation was purified to near homogeneity by ion exchange chromatography and exhibited maximal substrate specificity for amylose and efficiency in digesting various raw starches.

Extremely acidic beta-1,4-glucanase, CelA4, from thermoacidophilic Alicyclobacillus sp. A4 with high protease resistance and potential as a pig feed additive.

CelA4 was more stable, released more reducing sugar from barley beta-glucan, and under simulated gastric conditions, decreased the viscosity of barley-soybean feed to a greater extent, making it a good candidate as a new commercial glucanase to improve the nutrient bioavailability of pig feed.

Expression of Thermobifida fusca thermostable raw starch digesting alpha-amylase in Pichia pastoris and its application in raw sago starch hydrolysis

The purified amylase exhibited a high level of activity with raw sago starch and showed a single band at about 65 kDa by SDS-polyacrylamide gel electrophoresis after being treated with endo-β-N-acetylglycosaminidase H, which agrees with the predicted size based on the nucleotide sequence.

Raw-starch-digesting and thermostable alpha-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing.

A mutant AMY-CS2 that lacks the C-terminal domain lost not only its ability to bind or digest raw starch, but also its thermostability, so it is possible that the putative raw-starch-binding domain of AMY -CS2 plays a role not only in the molecule's raw-Starch-digesting ability but also in its ther mostability.