ArticleWorld journal of microbiology & biotechnology2017
The purification and characterization of a novel alkali-stable pectate lyase produced by Bacillus subtilis PB1.
Article in World journal of microbiology & biotechnology, 2017. 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, 32 citations in OpenAlex.
- Microbial production and biocatalytic docking of pectin lyase for green oil extraction in biorefinery applications.Archives of microbiology · 2026Article
- Review
- A Low-Temperature-Active Pectate Lyase from a Marine Bacterium for Orange Juice Clarification.Microorganisms · 2025Article
- Construction of pectinase gene engineering microbe and its application in tobacco sheets.Open life sciences · 2025Article
- Application of pectin hydrolyzing bacteria in tobacco to improve flue-cured tobacco quality.Frontiers in bioengineering and biotechnology · 2024Article
- Statistical bioprocess optimization for enhanced production of a thermo alkalophilic polygalacturonase (PGase) fromHeliyon · 2023Article
- Pectinase from a Fish Gut Bacterium, Aeromonas guangheii (SS6): Production, Cloning and Characterization.The protein journal · 2022Article
- Modification and application of highly active alkaline pectin lyase.AMB Express · 2022Article
- Screening of pectinase-producing bacteria from farmlands and optimization of enzyme production from selected strain by RSM.Folia microbiologica · 2020Article
- High copy number and highly stable Escherichia coli-Bacillus subtilis shuttle plasmids based on pWB980.Microbial cell factories · 2020Article
- Article
- High-Level Expression and Biochemical Properties of A Thermo-Alkaline Pectate Lyase FromFrontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pectinase is an important kind of enzyme with many industrial applications, among which pectinases produced by bacteria were scarce compared with fungal sources. In this study, a novel bacterium which produced extracellular pectinase was firstly isolated from flue-cured tobacco leaves and identified as Bacillus subtilis PB1 according to its 16S rRNA gene. The pectinolytic enzyme was purified by ammonium sulfate precipitation, ion-exchange and gel filtration chromatography, after which molecular weight was determined as 43.1 ± 0.5 kDa by SDS-PAGE. Peptide mass fingerprinting of the pectinase by MALDI-TOF MS showed that the purified enzyme shared homology with pectate lyase and was designated as BsPel-PB1. The optimal temperature for BsPel-PB1 was 50 °C. The optimal pH was pH 9.5 for BsPel-PB1 while it had a broad pH stability from 5 to 11. The values of K
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