ArticleIranian journal of pharmaceutical research : IJPR2015
Isolation and Characterization of a New Thermoalkalophilic Lipase from Soil Bacteria.
Article in Iranian journal of pharmaceutical research : IJPR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Microbial lipases: advances in production, purification, biochemical characterization, and multifaceted applications in industry and medicine.Microbial cell factories · 2025Review
- DIVERISTY and enzymatic potential of indigenous bacteria from unexplored contaminted soils in Faisalabad.Heliyon · 2023Article
- Protective effect of bacterial lipase on lipopolysaccharide-induced toxicity in rat cardiomyocytes; H9C2 cell line.Journal of cardiovascular and thoracic research · 2020Article
- Article
- Realm of Thermoalkaline Lipases in Bioprocess Commodities.Journal of lipids · 2018Review
- Enhanced Production and Characterization of a Highly Stable Extracellular Protease from an Extreme Halophilic IsolateIranian journal of pharmaceutical research : IJPR · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipases are diversified enzymes in their properties and substrate specificity, which make them attractive tools for various industrial applications. In this study, an alkalinethermostable lipase producing bacteria were isolated from soil of different regions of Isfahan province (Iran) and its lipase was purified by ammonium sulfate precipitation and ion exchange chromatography. To select a thermoalkalophil lipase producing bacterium, Rhodamine B and Horikoshi media were used and the strain that can grow at 45° Cwas selected. The isolated strain was identified using microbial and biochemical tests. One strain showed an orange colored zone on plate and grew on Horikoshi plate. Microbial and biochemical tests showed that the isolated strain was Bacillus subtilis, a Gram positive rod. In PCR, an expected band was obtained with about 371 bp. The activity of the purified lipase was 10.2 folds that of the standard enzyme using ammonium sulfate precipitation and ion exchange chromatography. The molecular weight of lipase determined by SDS-PAGE electrophoresis, was 21 and 35 KDa. Existence of two bands in SDS-PAGE electrophoresis and low amount of obtained purified enzyme highlights the necessity of optimization of purification and concentrating process.
Indexed as
Identifiers
26330879PMC4518119W1956328498What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.