Rapid Zymogram for Lipase

Rp, Yadav; Rk, Saxena; Gupta, Rani; Ws, Davidson

doi:10.2144/98245bm13

Cited by 13 publications

(15 citation statements)

References 5 publications

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“…Depending on its ionic characteristics, a detergent can be categorized as ionic, non-ionic or zwitterionic. The diverse effect of surfactants and solvents on enzyme activities of esterases and lipases from various sources was reported previously in the liter- ature [45][46][47][48][49][50][51][52][53]. We test the effects of ionic (SDS), non-ionic (tween 80 and triton X-100), and zwitterionic (CHAPS) surfactants on the enzyme activity.…”

Section: Compoundmentioning

confidence: 96%

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Fazary

Ismadji

2009

International Journal of Biological Macromolecules

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Section: Compoundmentioning

confidence: 96%

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Fazary

Ismadji

2009

International Journal of Biological Macromolecules

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“…SDS was often noted by other authors to more or less depress the activity of lipolytic enzymes [8,9,24]. Sodium cholate Table 1…”

Section: Resultsmentioning

confidence: 93%

“…mendocina 3121-1 lipase could be attributed to lipolytic enzymes specific of long-chain unsaturated TAGs. Most of lipases have been shown to be specific for TAGs of a moderate chain length [8,[16][17][18][19]. According to such results, we investigated the hydrolysis of Tween 85 (polyoxyethylenesorbitan trioleate) in a wide range of the detergent concentrations.…”

Section: Resultsmentioning

confidence: 99%

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Tween'ų ir joninių detergentų poveikis hidroliziniam <i>Pseudomonas mendocina</i> 3121-1 lipazės aktyvumui

Bendikienė¹,

Surinėnaitė²,

Bachmatova³

et al. 2008

Biologija

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A more detailed analysis of Pseudomonas mendocina 3121-1 lipase catalytic activity in hydrolysing non-ionic detergents Tweens was the goal of the present study. Tweens as lipase substrates were used in aqueous media at the following final concentrations: half of the critical micelle concentration (CMC), close to CMC, five-fold above CMC and by far exceeding CMC (11-44 mM). The intensity of the hydrolysis of the detergents increased with increasing fatty acid chain length in the Tween structure. The reaction rate also depended on the detergent concentration and changed (increased) at the point when it exceeded the CMC, suggesting that Tweens at those concentrations are not well suitable for stabilizing the Ps. mendocina lipase substrate emulsion.The role of ionic detergents in the lipase-catalysed hydrolysis of soluble substrate p-nitrophenyl butyrate (p-NPB) was also investigated. The hydrolytic activity was shown to be rapidly declined by sodium dodecylsulphate (SDS) during the first 10 min, slower inactivated by dodecyltrimethylammonium bromide (DTMAB) and only slightly affected by sodium deoxycholate (SDCh). The inactivation rate constants (k inact , min -1 ) were calculated to be 0.29, 0.07 and 0.006 for SDS, DTMAB and SDCh, respectively.

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“…It is known that there are certain lipases or esterases whose activities are enhanced by Mg 2þ , 25,26) but there have been hardly any reports on Mg 2þ -specific inhibition of lipase or esterase. Inhibition of YvdO might be due to a critical change near its active site, which is induced by Mg 2þ binding, suggesting that the enzyme has a specific binding site for Mg 2þ .…”

Section: Discussionmentioning

confidence: 99%

Biochemical Analysis of a Novel Lipolytic Enzyme YvdO fromBacillus subtilis168

Kato

Yoshimura

Hemmi

et al. 2010

Bioscience, Biotechnology, and Biochemistry

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The predicted amino acid sequence of Bacillus subtilis yvdO exhibits similarity to that of the proteins belonging to the patatin family of lipolytic enzymes. In the present study, YvdO was overproduced in Escherichia coli and purified, and its enzymatic properties were determined. YvdO hydrolyzed p-nitrophenyl fatty acid esters. The enzyme was specific to middle-chain fatty acids, and its optimum pH was approximately 7.5. It maintained 86% of its initial activity after incubation for 30 min at 80 degrees C, and its secondary structure was retained at up to 80 degrees C. Free myristic acid was detected as the product of the reaction with YvdO and 1-myristoly-2-lyso-sn-glycero-3-phosphocholine, while YvdO did not hydrolyze 1,2-dimyristoly-sn-glycero-3-phosphocholine. These results suggest that YvdO is a novel thermostable lipolytic enzyme that has the ability to hydrolyze lysophospholipids.

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Rapid Zymogram for Lipase

Cited by 13 publications

References 5 publications

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Tween'ų ir joninių detergentų poveikis hidroliziniam <i>Pseudomonas mendocina</i> 3121-1 lipazės aktyvumui

Biochemical Analysis of a Novel Lipolytic Enzyme YvdO fromBacillus subtilis168

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