Production, purification and biochemical characterisation of a novel lipase from a newly identified lipolytic bacterium <i>Staphylococcus caprae</i> NCU S6

Zhao, Junsan; Ma, Maomao; Zeng, Zheling; Yu, Ping; Gong, Deming; Deng, Shuguang

doi:10.1080/14756366.2020.1861607

Cited by 38 publications

(18 citation statements)

References 34 publications

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“…fluorescens NS2W (24.5 U mL -1 ) [ 39 ]. Peptone was reported to be the best nitrogen source for lipase production from Serratia marcescens (28.5 UmL -1 ) [ 11 ] and 1% yeast extract for Bacillus glycinifermentans MK-840989 (16.8 UmL -1 ) [ 40 ]. Yeast extract was also found as the best nitrogen source for lipase activity by Lysinibacillus PL33 (400 U mL -1 ) followed by Lysinibacillus PL35 (380 U mL -1 ), Bacillus L8 (350 U mL -1 ), Bacillus FW2 (290 U mL -1 ), Bacillus N-PL4 (260 U mL -1 ), and Paenibacillus L2 (220 U mL -1 ).…”

Section: Resultsmentioning

confidence: 99%

“…The most influential criteria to produce lipase are dietary factors, including carbon and nitrogen sources. Bacterial lipases are generally active over a wide pH range (pH 3.0–12.0) [ 11 ], while temperature optima ranges from 30–60°C. Some essential bacterial genera that produce industrial lipases include Bacillus , Pseudomonas , and Acinetobacter .…”

Section: Introductionmentioning

confidence: 99%

“…is the major source, producing a variety of soluble extracellular enzymes. These strains are commercially essential industrial extracellular enzyme producers and can be cultured under extreme temperature (40-60˚C) and pH (9)(10)(11) conditions to produce products that are, in turn, stable in a wide range of harsh environments [12]. Because of the tremendous properties and applications of lipolytic enzymes produced from bacterial strains, especially Bacillus sp, it is paramount to identify highly enzymatic bacteria.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2022

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2022

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“…The tolerance of an enzyme to various metal ions plays a major role in industrial applications. 34 The effects of metal ions on tannase activity (NCUF M8 and NCUF FCYN212) were studied at concentrations of 1 and 10 mmol L −1 (Table 1). K + and Zn 2+ significantly increased the tannase activity at 1 mmol L −1 .…”

Section: Effect Of Metal Ions On Tannase Activitymentioning

confidence: 99%

Molecular mechanism of high‐production tannase of Aspergillus carbonariusNCUF M8 after ARTP mutagenesis: revealed by RNA‐seq and molecular docking

et al. 2022

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BACKGROUND Tannase is an enzyme produced by microbial fermentation and is widely used in the food industry; however, the molecular mechanism of tannase production by Aspergillus has not yet been studied. This study was conducted to reveal the differences in Aspergillus carbonarius tannase enzymatic characterization, secondary structures and molecular mechanisms after treatment of the strain with atmospheric and room temperature plasma (ARTP). RESULTS The results showed that the specific activity of tannase was improved by ARTP treatment, and it showed higher thermostability and tolerance to metal ions and additives. The enzymatic characterization and molecular docking results indicated that tannase had a higher affinity and catalytic rate with tannic acid as a substrate after ARTP treatment. In addition, the docking results indicated that Aspergillus tannases may catalyze tannic acid by forming two hydrogen‐bonding networks with neighboring residues. RNA‐seq analysis indicated that changes in steroid biosynthesis, glutathione metabolism, glycerolipid metabolism, oxidative phosphorylation pathway and mitogen‐activated protein kinase signaling pathways might be crucial reasons for the high production of tannase. CONCLUSION ARTP enhanced the yield and properties of A. carbonarius tannase by changing the enzyme structure and cell metabolism. This study provides a theoretical basis for elucidating the molecular mechanism underlying high production of Aspergillus tannases. © 2022 Society of Chemical Industry.

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“…Lipolytic enzymes are widely distributed in nature (i.e., animals, plants, and microorganisms), and a relatively large number has been isolated from metagenomes and bacteria [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ]. The latter includes enzymes with different biological activities isolated from genera such as Pseudomonas [ 1 ], Psychrobacter [ 5 ], Salinisphaera [ 9 ], Serratia [ 11 ], Burkholderia [ 12 ], and Staphylococcus [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses.

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Production, purification and biochemical characterisation of a novel lipase from a newly identified lipolytic bacterium Staphylococcus caprae NCU S6

Cited by 38 publications

References 34 publications

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

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

Molecular mechanism of high‐production tannase of Aspergillus carbonariusNCUF M8 after ARTP mutagenesis: revealed by RNA‐seq and molecular docking

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

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