Stabilization of Bacillus licheniformis α-amylase by specific antibody which recognizes the N-terminal fragment of the enzyme

Ghasemi, Ali; Khajeh, Khosro; Ranjbar, Bijan

doi:10.1016/j.ijbiomac.2007.01.012

Cited by 2 publications

(1 citation statement)

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“…They are registered in the SWISS-PROT database as AMY_BACAM, AMY_BA-CLI, AMYM_BACLI, and AMY_BACSU. Ghasemi et al (2007) reported the generation and identification of two large polypeptides after trypsin digestion and SDS-PAGE analysis of the a-amylase from B. licheniformis. N-terminal sequencing of the peptides after purification by SDS-PAGE revealed that trypsin cleaved the Arg127-Val128 peptide bond.…”

Section: Products From Bacillus Spmentioning

confidence: 99%

Classification of microbial α‐amylases for food manufacturing using proteinase digestion

Akiyama

Yamazaki

Tada

et al. 2014

Food Science & Nutrition

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Enzymes produced by microorganisms and plants are used as food additives to aid the processing of foods. Identification of the origin of these enzyme products is important for their proper use. Proteinase digestion of α-amylase products, followed by high performance liquid chromatography (HPLC) analysis, was applied to α-amylase from the mold Aspergillus species, the bacteria Bacillus species, and the actinomycetes Saccharomonospora species. Eighteen commercial products of α-amylase were digested with trypsin and endoproteinase Lys-C and HPLC analyzed. For some proteinase/sample combinations, the area of the intact α-amylase peak decreased and new peaks were detected after digestion. The presence and retention times of the novel peaks were used to group the products. The results from this method, called the proteinase digestion–HPLC method, allowed the classification of the α-amylase products into 10 groups, whereas the results from sodium dodecyl sulfate polyacrylamide gel electrophoresis allowed their classification into seven groups.

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Section: Products From Bacillus Spmentioning

confidence: 99%