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

@article{Bai2012IdentificationOA,
  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},
  year={2012},
  volume={131},
  pages={1473-1478}
}

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TLDR
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

TLDR
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

TLDR
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.

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TLDR
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TLDR
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

TLDR
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.

TLDR
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