ArticleJournal of industrial microbiology & biotechnology2013
Purification, characterization and cloning of a thermotolerant isoamylase produced from Bacillus sp. CICIM 304.
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 40 citations in OpenAlex.
- A novel multifunctional starch debranching enzyme from Myxococcus sp. V11.Applied microbiology and biotechnology · 2026Article
- Superior thermostability and divalent cation sensitivity of isoamylase CMI294C from Cyanidioschyzon merolae.Plant molecular biology · 2025Article
- Effect of Non-Foods (Basel, Switzerland) · 2025Article
- Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) fromFoods (Basel, Switzerland) · 2024Article
- Review
- Proteomic perspectives on thermotolerant microbes: an updated review.Molecular biology reports · 2022Review
- Insufficiency in functional genomics studies, data, and applications: A case study of bio-prospecting research in ruminant microbiome.Frontiers in genetics · 2022Review
- Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.Applied microbiology and biotechnology · 2019Article
- A systematic optimization of styrene biosynthesis inBiotechnology for biofuels · 2018Article
- Engineering of isoamylase: improvement of protein stability and catalytic efficiency through semi-rational design.Journal of industrial microbiology & biotechnology · 2016Article
- Doubling Power Output of Starch Biobattery Treated by the Most Thermostable Isoamylase from an Archaeon Sulfolobus tokodaii.Scientific reports · 2015Article
- Microbial enzymes with special characteristics for biotechnological applications.Biomolecules · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel thermostable isoamylase, IAM, was purified to homogeneity from the newly isolated thermophilic bacterium Bacillus sp. CICIM 304. The purified monomeric protein with an estimated molecular mass of 100 kDa displayed its optimal temperature and pH at 70 °C and 6.0, respectively, with excellent thermostability between 30 and 70 °C and pH values from 5.5 to 9.0. Under the conditions of temperature 50 °C and pH 6.0, the K m and V max on glycogen were 0.403 ± 0.018 mg/mg and 0.018 ± 0.001 mg/(min mg), respectively. Gene encoding IAM, BsIam was identified from genomic DNA sequence with inverse PCRs. The open reading frame of the BsIam gene was 2,655 base pairs long and encoded a polypeptide of 885 amino acids with a calculated molecular mass of 101,155 Da. The deduced amino acid sequence of IAM shared less than 40 % homology with that of microbial isoamylase ever reported, which indicated it was a novel isoamylase. This enzyme showed its obvious superiority in the industrial starch conversion process.
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