Purification and characterization of two distinct thermostable lipases from the gram-positive thermophilic bacterium Bacillus thermoleovorans ID-1

Lee, Dong Woo; Kim, Hack Woo; Lee, Moon Hyoung; Kim, Byoung Chan; Choe, Eun Ah; Lee, Han Seung; Kim, Doo Sik; Pyun, Yu‐Ryang

doi:10.1016/s0141-0229(01)00408-2

Cited by 77 publications

(55 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…EDTA treatment strongly inhibited the lipase activity with the increasing concentrations confirming that B. smithii lipase requires metal ions for their activity. Similar result was reported for B. thermolevorans ID-1 lipase (Lee et al 2001). Unlike most other bacterial lipases, the B. smithii lipase was observed to be a metallo-enzyme inhibited by EDTA as well as PMSF.…”

Section: Discussionsupporting

confidence: 86%

“…Further, the results obtained indicated clearly that the enzyme is thermostable in nature and can tolerate higher temperatures above 50°C. In fact temperature optimum of 45°C and above has been reported for lipases isolated from many Bacillus species (Lee et al 2001;Jinwal et al 2003). Most of the industrial processes involving enzymes operate at temperatures above 50°C, and consequently thermostable enzymes assume great significance (Sharma et al 2002).…”

Section: Discussionmentioning

confidence: 99%

“…A comparison of the chromatogram obtained for the hydrolytic products of triolein from thin layer chromatography (TLC) with that of BTID-A Bacillus lipase (Lee et al 2001) indicated that 1,2-and 1,3-diolein and monoolein were released as the main products by B. smithii Microbiol Biotechnol (2013) 29:1349-13601357 lipase and the enzyme is likely to be positionally nonregiospecific. Further, this observation also indicated that this enzyme may probably act synergistically to hydrolyze extracellular lipids to free fatty acids and glycerols.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

View full text Add to dashboard Cite

Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50°C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30-80°C) and pH (7.0-10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries.

show abstract

Section: Discussionsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…These values are close to the optima reported for Bacillus thermoleovorans ID-1 lipases [4,18], for Bacillus thermocatenulatus lipases [5,18], for the lipase produced by Thermoactinomyces vulgaris [6] and the lipase produced by Bacillus circulans [21].…”

Section: Enzyme Characterisationsupporting

confidence: 86%

“…Enzyme activity as a function of temperature was studied by incubating the p-nitrophenyl laurate reaction vessels at different temperatures (18,30,40, 55, 60, 65 and 70 C).…”

Section: Partial Characterisation Of the Lipasementioning

confidence: 99%

A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

Al-Khudary

Hashwa²,

Mroueh

2004

Engineering in Life Sciences

View full text Add to dashboard Cite

A filamentous, Gram-positive, spore forming aerobic bacterium was isolated from olive oil contaminated soil (Al Koura, Lebanon) on rhodamine agar plates at 60 C. The isolate, HRK-1 produced large quantities of an extracellular thermostable lipase which degrades olive oil. It was primarily classified as a Thermoactinomyces sp. due to the filamentous structure of its cells that bear one spore each on an un-branched sporophore, the resistance of its spores to boiling, utilisation of sucrose as a carbon source and production of dark pigments. The isolate grew optimally at a temperature of 60 C, a pH of 7.3 and an orbital shaking of 250 rpm. It showed an efficient olive oil degrading ability. No traces of triolein were detected after a 36-h cultivation. A concentration of 10 % [v/v] olive oil did not inhibit its growth. Lipase production was constitutive, and did not depend on the presence of olive oil. The optimum concentration of olive oil for lipase activity was 1 % [v/v], and the activity was not enhanced at higher concentrations, but on the contrary, a decrease in enzyme activity was recorded. The lipase of HRK-1 was preliminarily characterised in the crude cell-free supernatant with a specific activity of 0.14 U/mg. It has an optimum activity at 60 C and a pH of 8.0. This lipolytic enzyme showed resistance to boiling and to a wide range of metallic ions and inhibitors. The formation of this heat-stable lipase started in the early exponential growth phase, while a maximum extracellular enzyme activity was detected at the end of the decline phase, when most of the cells appeared as spherical spores. The exceptionally high activity of lipase (2.37 U/ml) produced by HRK-1 measured in the cell free supernatant clearly indicated the commercial importance of this isolate, especially after it showed great stability at elevated temperatures.

show abstract

Extremophiles for Hydrolytic Enzymes Productions: Biodiversity and Potential Biotechnological Applications

Kour

Rana

Kaur

et al. 2019

Bioprocessing for Biomolecules Production

View full text Add to dashboard Cite

Purification and characterization of two distinct thermostable lipases from the gram-positive thermophilic bacterium Bacillus thermoleovorans ID-1

Cited by 77 publications

References 29 publications

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

Extremophiles for Hydrolytic Enzymes Productions: Biodiversity and Potential Biotechnological Applications

Contact Info

Product

Resources

About