ArticleAMB Express2023
A molecular study on recombinant pullulanase type I from Metabacillus indicus.
Article in AMB Express, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Elucidating the catalytic mechanism of a previously undescribed carbohydrate esterase family 7 acetyl xylan esterase (LaCE7A).The FEBS journal · 2026Article
- Characterization of Novel Pullulanase Type I from Newly Isolated Bacillus cereus Strain NP9: Potential Additive for Laundry Detergent Formulations.Applied biochemistry and biotechnology · 2025Article
- In silico and structural analysis of Bacillus licheniformis FAO.CP7 pullulanase isolated from cocoa (Theobroma cacao L.) pod waste.BMC microbiology · 2025Article
- Atomic-level binding interaction analysis ofIn silico pharmacology · 2025Article
- Extracellular Overexpression of a Neutral Pullulanase inBioengineering (Basel, Switzerland) · 2024Article
- Draft genome sequence ofMicrobiology resource announcements · 2024Article
- Isolation, characterization, and cloning of thermostable pullulanase fromSaudi journal of biological sciences · 2024Article
- Identification and characterization of a versatile keratinase, KerZJ, from Stenotrophomonas sp. LMY.World journal of microbiology & biotechnology · 2023Article
- Correction: A molecular study on recombinant pullulanase type I from Metabacillus indicus.AMB Express · 2023Article
- Pullulanase: unleashing the power of enzyme with a promising future in the food industry.Frontiers in bioengineering and biotechnology · 2023Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the great potential of cold-adapted pullulanase type I in tremendous industrial applications, the majority of commercialized pullulnases type I are of mesophilic and thermophilic origin so far. Hence, the present study underlines cloning, heterologous expression in Escherichia coli, characterization, and in silico structural modeling of Metabacillus indicus open reading frame of cold-adapted pullulanase type I (Pull_Met: 2133 bp & 710 a.a) for the first time ever. The predicted Pull_Met tertiary structure by I-TASSER, was structurally similar to PDB 2E9B pullulanase of Bacillus subtilis. Purified to homogeneity Pull_Met showed specific activity (667.6 U/mg), fold purification (31.7), molecular mass (79.1 kDa), monomeric subunit and Km (2.63 mg/mL) on pullulan. Pull_Met had optimal pH (6.0) and temperature (40
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