2011
DOI: 10.1590/s0101-20612011000300009
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Lipase and esterase: to what extent can this classification be applied accurately?

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Cited by 84 publications
(59 citation statements)
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References 36 publications
(23 reference statements)
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“…However, lipases are generally produced using lipidic carbon sources such as oils, fatty acids and glycerol [23] Two groups of hydrolases are lipases (EC 3.1.1.3) and esterases (EC 3.1.1.1), and these enzymes are differentiated according to their substrate specificity [24]. Lipases primarily act on water-insoluble substrates, such as triglycerides composed of long-chain fatty acids, whereas esterases preferentially hydrolyze 'simple' esters and typically act on only triglycerides composed of fatty acid chains shorter than C6 [25]. Lipase is an important enzyme that is used in biotechnological applications.…”
Section: Discussionmentioning
confidence: 99%
“…However, lipases are generally produced using lipidic carbon sources such as oils, fatty acids and glycerol [23] Two groups of hydrolases are lipases (EC 3.1.1.3) and esterases (EC 3.1.1.1), and these enzymes are differentiated according to their substrate specificity [24]. Lipases primarily act on water-insoluble substrates, such as triglycerides composed of long-chain fatty acids, whereas esterases preferentially hydrolyze 'simple' esters and typically act on only triglycerides composed of fatty acid chains shorter than C6 [25]. Lipase is an important enzyme that is used in biotechnological applications.…”
Section: Discussionmentioning
confidence: 99%
“…() and Lopes et al . (). Enzyme aliquot (0.070 mL) was added to 3.43 mL of reaction mixture containing 1.12 m m pNPB in 50 m m phosphate buffer pH 7.2 added of 0.2% (w/v) Triton X‐100 and 0.43 m tetrahydrofuran.…”
Section: Methodsmentioning
confidence: 97%
“…() and Lopes et al . (). The reaction mixture containing 0.9 mL substrate solution, 0.1 mL 50 m m phosphate buffer and 0.1 mL of enzyme was incubated at 37 °C for 30 min.…”
Section: Methodsmentioning
confidence: 97%
“…During fungi cultivation, and at regular 24 h intervals, samples were withdrawn and assayed for lipase activity. It was measured according to the method of Lopes et al (2011) [31], using the quantitative assay by titration of the liberated fatty acids after contact between enzymes and the substrate (triglyceride emulsion). Liberated fatty acids were immediately titrated by NaOH solution (0.05 M).…”
Section: Whole-cell Lipase-catalyzed Transesterificationmentioning
confidence: 99%