Regioselectivity of New Bacterial Lipases Determined by Hydrolysis of Triolein

Lanser, A. C.; Manthey, Linda K.; Hou, Ching T.

doi:10.1007/s00284-001-0019-3

Cited by 45 publications

(15 citation statements)

References 12 publications

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“…The results obtained are in agreement with that reported by Gulati et al (2005) where peptone was found to be the best nitrogenous source for lipase production. Similar findings were also reported in other Bacillus sp (8, 21, 34, 38 12). The lipase production was found to be low with soybean meal and corn steep liquor, whereas in other organic and inorganic nitrogen sources the lipase production was in the range of 10–17 U/ml.…”

Section: Resultssupporting

confidence: 91%

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic Bacillus sp isolated from Hotspring of Arunachal Pradesh, India

Bora¹,

Bora²

2012

Braz. J. Microbiol.

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Studies on lipase production were carried out with a bacterial strain (Bacillus sp LBN 2) isolated from soil sample of hotspring of Arunachal Pradesh, India. The cells were cultivated in a mineral medium with maximum production at 1% groundnut oil. The optimum temperature and initial medium pH for lipase production by the organism were 500C and 9.0 respectively. The molecular mass was found to be 33KDa by SDS PAGE. The optimal pH and temperature for activity were 10 and 600C respectively. The enzyme was found to be stable in the pH range of 8–11 with 90% retention of activity at pH 11. The enzyme retained 90% activity at 600C and 70% of activity at 700C for 1h. The lipase was found to be stable in acetone followed by ethanol. The present findings suggested the enzyme to be thermophilic alkaline lipase.

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Section: Resultssupporting

confidence: 91%

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic Bacillus sp isolated from Hotspring of Arunachal Pradesh, India

Bora¹,

Bora²

2012

Braz. J. Microbiol.

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“…DeAlmeida et al (2016) has earlier shown lipase production by various substrates individually, and after mixing with oils like olive oil. In the present experiment, the best nitrogen sources were peptone and yeast extract, similar to the results shown by Hasan et al (2001 (Oh et al, 1999;Ghanem et al, 2000;Lanser et al, 2002;Sharma et al, 2002), while tryptone and yeast extract have been used for S. haemolyticus L62 (Oh et al, 1999).…”

Section: Discussionsupporting

confidence: 87%

Optimized production of lipase from Bacillus subtilis PCSIRNL-39

Mazhar¹,

Abbas²,

Ali³

et al. 2017

Afr. J. Biotechnol.

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Lipases catalyze the hydrolysis of long chain triglycerides. Microbial lipases are receiving much attention because of their industrial potential in the chemical, pharmaceutical, medical, cosmetic, biosurfactant synthesis, leather industries, mutation, agrochemicals and paper manufacturing industries. This article presents the isolation of maximum lipase producing bacteria and the optimization of different conditions for the maximum production of lipase. Bacillus subtilis PCSIRNL-39 shows maximum production of lipase at 45°C with pH 7 using nitrogen source peptone and carbon source sucrose. B. subtilis PCSIRNL-39 showed the best production at 5% inoculum size, while Ca 2+ and Mg 2+ were found best stimulator for enzyme production during the study. Tween 20 and 80 enhanced better lipase production than other surfactant. The kinetic parameters of V max and K m for the lipase were measured to be 101 µM/min.mL and 7.6 mg, respectively.

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“…This species was able to prevent excessive hydration due to its ability to synthesize a nonspecific polysaccharide. In addition, a lipase activity of possible commercial value is produced by P. mucidolens (Lanser et al 2002). Despite its role in food spoilage and its possible commercial applications, control of its nucleic acid metabolism has not been studied.…”

Section: Introductionmentioning

confidence: 99%

Regulation of the Pyrimidine Biosynthetic Pathway in Pseudomonas mucidolens

West

2005

Antonie Van Leeuwenhoek

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Control of pyrimidine biosynthesis was examined in Pseudomonas mucidolens ATCC 4685 and the five de novo pyrimidine biosynthetic enzyme activities unique to this pathway were influenced by pyrimidine supplementation in cells grown on glucose or succinate as a carbon source. When uracil was supplemented to glucose-grown ATCC 4685 cells, activities of four de novo enzymes were depressed which indicated possible repression of enzyme synthesis. To learn whether the pathway was repressible, pyrimidine limitation experiments were conducted using an orotate phosphoribosyltransferase (pyrE) mutant strain identified in this study. Compared to excess uracil growth conditions for the glucose-grown mutant strain cells, pyrimidine limitation of this strain caused aspartate transcarbamoylase, dihydroorotase and dihydroorotate dehydrogenase activities to increase by more than 3-fold while OMP decarboxylase activity increased by 2.7-fold. The syntheses of the de novo enzymes appeared to be regulated by pyrimidines. At the level of enzyme activity, aspartate transcarbamoylase activity in P. mucidolens ATCC 4685 was subject to inhibition at saturating substrate concentrations. Transcarbamoylase activity was strongly inhibited by UTP, ADP, ATP, GTP and pyrophosphate.

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Regioselectivity of New Bacterial Lipases Determined by Hydrolysis of Triolein

Cited by 45 publications

References 12 publications

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic Bacillus sp isolated from Hotspring of Arunachal Pradesh, India

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic Bacillus sp isolated from Hotspring of Arunachal Pradesh, India

Optimized production of lipase from Bacillus subtilis PCSIRNL-39

Regulation of the Pyrimidine Biosynthetic Pathway in Pseudomonas mucidolens

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