Optimization Study of Lipolytic Enzyme from Bacillus cereus, PCSIR NL-37

Mazhar, Haniya; Abbas, Naaz; Zamir, Tehseen; Hussain, Zahid; Ali, Syed Shahid

doi:10.17582/journal.pujz/2018.33.2.217.224

Cited by 9 publications

(4 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This had also a positive effect on the dry weight of the mycelial biomass obtained on all three media (Table 2). Some studies have described a positive effect of Ca 2+ ions increasing the biosynthesis of lipases, e.g., lipases from Bacillus cereus [44] and Penicillium camemberti [45]. However, in this study, the increase in lipase biosynthesis by C. pannorum A-1 does not seem to be caused directly by Ca 2+ ions, because there were no significant differences in the activities between the BMC and BM media (without olive oil and glucose).…”

Section: Discussioncontrasting

confidence: 74%

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

et al. 2021

View full text Add to dashboard Cite

A biomass-bound lipase from psychrophilic Chrysosporium pannorum A-1 is an efficient biocatalyst for direct esterification of β-citronellol and acetic acid in an organic solvent. The biomass is effectively produced by fungal submerged culture at 20 ℃, which results in lower energy consumption during the production of biocatalyst. Supplementation of the culture medium with calcium carbonate together with olive oil contributed to a significant increase in the active biomass of mycelium in one batch culture and increased the efficiency of the biocatalyst. Biomass-bound lipase showed high catalytic activity in a broad temperature range of 30–60 °C and stability up to 70 °C. A maximum molar conversion value of 98% was obtained at 30 °C in n-hexane using a 2:1 alcohol-to-acid molar ratio and 3% w/v of the biocatalyst within 24 h. The high equimolar concentration of the substrates (200 mM) did not have an adverse effect on mycelial biomass activity. Dry mycelium of C. pannorum is a promising biocatalyst for large-scale biosynthesis of citronellyl acetate, given its low-cost production, high activity at low temperatures, and reusability in a minimum of seven 24-h biocatalytic cycles.

show abstract

Section: Discussioncontrasting

confidence: 74%

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Maltose and yeast extract were reported previously which enhanced lipase production with the lipolytic activity of 30.17 UmL -1 and 50.83 UmL -1 from Bacillus cereus , PCSIR NL-37 [ 31 ]. Starch enhanced the production of lipase enzyme from Serratia rubidaea with enzyme activity of 15.60±0.20 UmL -1 [ 32 ] whereas sucrose and fructose enhanced lipolytic activity with 40.67 UmL -1 and 31.70 UmL -1 respectively from Bacillus subtilis PCSIRNL-39 [ 33 ]. Lipase production was stimulated in the presence of glucose from bacillus FW2 (230 UmL -1 ).…”

Section: Resultsmentioning

confidence: 99%

Optimization and characterization of alkaliphilic lipase from a novel Bacillus cereus NC7401 strain isolated from diesel fuel polluted soil

et al. 2022

View full text Add to dashboard Cite

Five Bacillus cereus strains including B. cereus AVP12, B. cereus NC7401, B. cereus BDBCO1, B. cereus JF70 and B. specie JL47 isolated from the diesel fuel polluted soil adhered to the roots of Tagetes minuta were screened for lipase production with phenol red agar method. B. cereus NC7401 strain successfully expressing and secreting lipase with maximal lipolytic activity was subjected to a submerged fermentation process with five different carbon (starch, glucose, maltose, fructose, and lactose) and five different nitrogen (tryptone, ammonium nitrate, peptone, urea, yeast extract) sources to produce lipase enzyme. Maximum enzyme activity was found with starch (30.6 UmL-1), maltose (40 UmL-1), and tryptone (38.6 UmL-1), and the lipases produced using these sources were named lipase A, B, and C respectively. The total protein content of 8.56, 8.86, and 2.75 μg mL-1 were obtained from B. cereus NC7401 cultured using starch, maltose, and tryptone respectively. Lipase was stable between temperature range 30–80°C and pH 5–10 whereas optimally active at 55°C and pH 8.0. The enzyme was relatively stable for 10 days at 4°C and its optimum reaction time with the substrate was 30 minutes. It was tolerant to 1.5% (v/v) methanol as an organic solvent, 1.5% (v/v) Triton X-100 as a media additive and 1.5% (w/v) Ni2+ as a metal ion. SDS, n-hexane, and Ag+ inhibited lipolytic activity. Oil stains were removed from cotton fabric which showed oil removal efficiency enhancement in the presence of a lipase. Fat hydrolysis of 20, 24, and 30% was achieved following 6 hours of incubation of the fat particles with lipase A, B, and C respectively at a concentration of 20 mg mL-1. To as best of our knowledge, this study on lipases extracted from bacteria of Azad Kashmir, Pakistan origin has never been reported before.

show abstract

“…The biofilm assay was carried out by using Mostafa et al ., method [102] . Virulence factors was analysed by reported methods such as staphyloxanthin assay – Hall [103] et al ., lipolytic assay – Mazhar [104] et al ., pyocyanin assay – Essar [70] et al ., Rhamnolipids assay –Marchant [105] et al ., proteolytic assay – Ganesh [106] et al ., and LasA assay – Kessler [73] et al ., methods respectively. Light microscopy analysis (40x magnification) method performed as previously reported methods on glass coverslips for Pseudomonas aeruginosa [107a,b] and Staphylococcus aureus [107c] …”

Section: Methodsmentioning

confidence: 99%

Anti‐Biofilm and Anti‐Virulence Potential of 2‐Amino‐1,3,4‐Thiadiazole Derivatives

Saravanan,

Venugopal,

Murugesan

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

Biofilms are microbial communities that facilitate the pathogenesis of life‐threatening microbial infections through the glazing of mucosal surfaces or implanted devices thus protecting them from medications and increasing mortality rates. To discover a new class of antibiofilm agents 2‐amino‐1,3,4 thiadiazoles hybridized with pharmacologically active heterocycles were designed and synthesized. The compounds were characterized by infrared, nuclear magnetic resonance, mass spectroscopy and elemental analysis. All the compounds were assessed for their anti‐biofilm and anti‐virulence activity against P. aeruginosa and S. aureus. Quinoline‐substituted thiadiazoles were found to possess potent anti‐biofilm activity against P. aeruginosa and S. aureus. The molecular docking analysis further confirms the antibiofilm potential of the compounds. Density functional theory studies were carried out to investigate the electronic and molecular properties of the most active hybrids.

show abstract

Optimization Study of Lipolytic Enzyme from Bacillus cereus, PCSIR NL-37

Cited by 9 publications

References 19 publications

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

Optimization and characterization of alkaliphilic lipase from a novel Bacillus cereus NC7401 strain isolated from diesel fuel polluted soil

Anti‐Biofilm and Anti‐Virulence Potential of 2‐Amino‐1,3,4‐Thiadiazole Derivatives

Contact Info

Product

Resources

About