Characterization of an extracellular lipase from the biocontrol fungus, Nomuraea rileyi MJ, and its toxicity toward Spodoptera litura

Supakdamrongkul, Piyaporn; Bhumiratana, Amaret; Wiwat, Chanpen

doi:10.1016/j.jip.2010.06.011

Cited by 52 publications

(35 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…al. (2016) 2+ and Cu 2+ with 60%, 69% and 75% relative activity respectively, which suggests that metal ions may be interfering with enzyme activity by acting directly on enzyme active site (Supakdamrongkul et. al., 2010).…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Lipase from <i>Aspergillus flavus</i> PW2961 using Magnetic Nanoparticles.

Kareem¹,

Adebayo²,

Balogun³

et al. 2017

Nig. J. Biotechnol

View full text Add to dashboard Cite

Lipase from Aspergillus flavus was purified in a single step purification using MnFeO 4 magnetic nano particles to achieve a 20.53-fold purification with specific activity of 11.29 U/mg and a 59% recovery yield. SDS-PAGE of lipase showed a single pure band with corresponding molecular weight of 35 kDa. The optimal temperature and pH for the enzyme activity were 45°C and 7.0 respectively. Addition of olive oil (1 %w/v) enhanced pH stability of the lipase with 86% residual activity at pH 7.0 after 6 h of incubation while the lipase was thermostable with 79% residual activity after 4 h of incubation. The enzyme activity was enhanced by Ca

show abstract

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Lipase from <i>Aspergillus flavus</i> PW2961 using Magnetic Nanoparticles.

Kareem¹,

Adebayo²,

Balogun³

et al. 2017

Nig. J. Biotechnol

View full text Add to dashboard Cite

show abstract

“…BPL was found to be stable at 100°C after 5-min of incubation, maintains about 60% of its activity. Proteins were precipitated by acetone (v/2v) and visualized by SDS-PAGE 15% (Figure 2b), Which is a special case in the world, until now no lipase supports a temperature of 70°C and 100°C [20,21,22].…”

Section: Methodsmentioning

confidence: 99%

Biochemical characterization of a new thermostable lipase from Bacillus pumilus strain

Faouzi

Bergadi

Sayari³

et al. 2015

Turk J Bioch

View full text Add to dashboard Cite

Objective: Research and characterization of new thermostable lipases from bacterial strains isolated from tannery waters in the old medina of Fez. Methods: Gene which encodes the 16S ribosomal RNA for a bacterial species was amplified via PCR and sequenced (Bacillus pumilus HF544325). The extracellular lipase from B. pumilus is purified by gel filtration (Sephacryl S-200) and cation exchange chromatography (Mono S sepharose cation exchanger). The N-terminal sequences of purified Bacillus pumilus lipase were determined by automated Edman's degradation, using an Applied Biosystems 470 A protein sequencer equipped with PTH 120A analyser. The activity of lipase was examined within the pH range of 6.0-10.0 and the effect of pH on lipase stability was determined by incubating the lipase fraction in various buffer solutions ranging from 3.0 to 10.0 for 24 h at room temperature. Results:The results showed that Bacillus pumilus is a strain that produce non-inducible lipase. This enzyme has a molecular weight of 27 kDa and presents a maximal activity at pH 8 and 45°C. The 18 N-terminal amino acid residues showed a high degree of homology with other Bacillus lipase sequences. After treatment in 100°C for 5 min, the thermostable enzyme maintains 60% of its activity, which is greater than that those founded in previous works. The enzyme retained 100% of its activity after 30 min incubation at 70°C. Conclusion: This newly isolated lipase is thermostable and it has a significant difference which was observed when the biochemical properties of the Bacillus pumilus lipase were compared to others microbial lipases. The Bacillus pumilus lipase can be considered as a good candidature for industrial and biotechnological applications. Key Words: Bacillus pumilus, lipase, purification, thermostable Conflict of Interest: The authors have no conflict of interest. ÖZETAmaç: Çalışmanın amacı Fez şehrinde bulunan tabakhane sularından izole edilen bakteri suşla-rından, sıcaklığa dayanıklı yeni bir lipaz enzimini saflaştırarak karakterize etmektir. Metod: Bakteri türleri için 16S ribosomal RNA'yı kodlayan gen PCR ile çoğaltılarak sekanslanmıştır (Bacillus pumilus HF544325). Ekstraselüler lipaz jel filtrasyonu (Sefakril S-200) ve katyon değiştirici kromatografi kullanılarak (Mono S Sefaroz katyon değiştirici) B. pumilus'den saflaştırılmıştır. Saflaştırılan Bacillus pumilus lipazının N-terminal dizisi Edman degredasyon yöntemi (Applied Biosystems 470 A protein sekanslama cihazı ile PTH120A analizör) ile saptanmıştır. Lipaz aktivitesi 6.0-10.0 pH aralığında incelenmiş, pH'nın lipaz enziminin dayanık-lılığına olan etkisi lipaz fraksiyonunu pH'sı 3.0 ile 10.0 arasında değişen çeşitli tampon çözel-tilerinde 24 saat oda sıcaklığında inkübe ederek araştırılmıştır. Bulgular: Sonuçlar Bacillus pumilus suşunun indüklenmeyen lipaz enzimini ürettiğini gös-termektedir. Lipaz enzimi 27 kDa molekül ağırlığına sahip olup, en yüksek aktiviteyi pH 8 ve 45°C'de göstermektedir. Amino ucundaki 18 amino asit diğer Bacillus lipaz dizileri ile yüksek oranda ...

show abstract

“…One is direct action at the catalytic site, as with many other enzymes whereas another is specific action resulting in the formation of complexes between the metal ions and ionised fatty acids in a manner that changes their solubility and behaviour at interfaces. 5 The effect of solvents on lipase activity is shown in Table 4, where all values were determined in triplicate with a coefficient of variation of less than 5%. Except for pyridine, all solvents acted as inhibitors, especially ethanol, isopropanol and acetone, which in high concentrations reduced activity by approximately 30, 20 and 12%, respectively.…”

Section: Effect Of Metal Ions and Solvents On Lipasementioning

confidence: 99%

“…3,4 Consequently, lipases have gained importance and been applied widely in various fields such as foods, pharmaceuticals, detergents, biosensors, biodiesel, cosmetics, fine chemicals and agrochemicals. 5 In view of their wide variety of applications, there has been renewed interest in the development of sources of lipases. They are widely distributed in nature in different organisms such as fungi, bacteria, plants and animals, and have been studied extensively for their properties.…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001

et al. 2012

View full text Add to dashboard Cite

Recebido em 26/9/11; aceito em 24/1/12; publicado na web em 15/5/12Lipases are characterised mainly by catalytic versatility and application in different industrial segments. The aim of this study was to biochemically characterise a lipase from a new strain of Bacillus sp. ITP-001. The isoelectric point and molecular mass were 3.12 and 54 kDa, respectively. The optima lipase activity was 276 U g -1 at pH 7.0 and a temperature of 80 °C, showing greater stability at pH 5.0 and 37 °C. , respectively determined by the Eadie-Scatchard method.

show abstract

Characterization of an extracellular lipase from the biocontrol fungus, Nomuraea rileyi MJ, and its toxicity toward Spodoptera litura

Cited by 52 publications

References 51 publications

Purification and Characterization of Lipase from <i>Aspergillus flavus</i> PW2961 using Magnetic Nanoparticles.

Purification and Characterization of Lipase from <i>Aspergillus flavus</i> PW2961 using Magnetic Nanoparticles.

Biochemical characterization of a new thermostable lipase from Bacillus pumilus strain

Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001

Contact Info

Product

Resources

About