Synergistic Effects of Surfactants on Kid Pregastric Lipase Catalyzed Hydrolysis Reactions

and, Douglas T. Lai; O’Connor, Charmian J.

doi:10.1021/la990618q

Cited by 11 publications

(6 citation statements)

References 19 publications

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“…Substrate and detergent interactions with lipases can be complex and unpredictable [ 25 , 29 - 31 ]. There have been a few studies involving the effect of detergents on lipase activity [ 20 , 32 , 33 ]. However, all these studies used p -nitrophenyl butyrate as substrate which is a common substrate for esterases.…”

Section: Resultsmentioning

confidence: 99%

Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica

Salameh¹,

Wiegel²

2010

Open Biochem J

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Thermosyntropha lipolytica DSM 11003, an anaerobic thermophilic lipolytic bacterium, produces the two alkalithermophilic lipases, LipA and LipB. Among all tested detergents, the two lipases were mostly affected by SDS when used at concentrations below its critical micelle concentration (CMC). In the absence of SDS, the vmax of both LipA and LipB were 12.6 U·mg-1 and 13.3 U·mg-1 and K0.5 were 1.8 mM and 1.65 mM, respectively at 96°C and pHopt25ºCof 9.4-9.6. In the presence of 0.2% SDS, the vmax increased to 105 U·mg-1 and 112 U·mg-1, and K0.5 values decreased to 200 µM and 140 µM for LipA and LipB, respectively. Inhibitory assays of lipases using diisopropyl p-nitrophenylphosphate (E600) with increasing concentration of SDS and Tween 20 strongly suggest that SDS and Tween 20 do bind to the lid domain and/or active site pocket, thus promoting conformational changes that facilitate active site accessibility for the substrate. The two lipases exhibited moderate activation in the presence of nonionic detergents when used below their CMC values. Both lipases were found to exhibit strong tendency to aggregate as observed through gel filtration chromatography and gradient native gel electrophoresis. The addition of 1.0% (w/v) SDS led to disaggregation as the lipases were eluted corresponding to their monomeric mass (based on SDS gel electrophoresis value) and caused a significant decrease in thermostability, suggesting that, enzyme aggregation might be a major contributor to the high thermostability of LipA and LipB.

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Section: Resultsmentioning

confidence: 99%

Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica

Salameh¹,

Wiegel²

2010

Open Biochem J

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“…Moreover, surfactants had a positive effect on the interaction between enzyme and substrate. [27,28] In this experiment, the selected surfactants were sodium stearoyl lactylate (SSL), calcium stearyl lactylate (CSL), Tween-80, and Span-60. Each amount of the surfactants was added to about 0.5% (w/w).…”

Section: Effect Of Different Surfactants Additionmentioning

confidence: 99%

Surfactant-assisted enzymatic extraction of piperine from Piper nigrum L

Yang

et al. 2020

International Journal of Food Properties

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Surfactant-assisted enzymatic hydrolysis was used to extract the flavor compounds from piper nigrum L. The extraction conditions were optimized through orthogonal and single-factor experiments. The extracted piperine content, measured with High-Performance Liquid Chromatography (HPLC) and UV spectrophotometric, was used as experimental index. The optimized conditions were as follows: the amount of cellulase, neutral protease and surfactant (sodium stearoyl lactylate) addition was 0.08%, 0.1% and 0.4% (w/w) respectively. The solid-liquid ratio was 1:5 (g/mL), the enzymolysis temperature and time were 60°C and 4 h, and the granularity was less than 10 mesh. Under these conditions, the content of the extracted piperine was 4.54% (UV spectrophotometric) and 4.42% (HPLC), respectively. Meanwhile, the mechanisms of the enzymatic reaction, as well as the role of the surfactant in enzymatic hydrolysis process were discussed.

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“…In the micelles formed by bile salts, the hydrophobic faces are considered to be in contact with each other while the hydrophilic faces are directed to the aqueous environment. [28][29][30] In this sense, an important difference between the sodium deoxycholate and the other two bile salts [31] 7-16.2 [35] Sodium deoxycholate 0.69 AE 0.005 3-10 [31] 2-4 [35,36] CHAPS 1.24 AE 0.008 6.5 [35] Triton X-100 0.14 AE 0.001 0.25 [35] 0.3-0.6 [37] used in this work is the removal of one hydroxyl group in the a-face (Table 2) that causes an increase in the overall hydrophobicity of the sodium deoxycholate micelles. [31] We suggest that this situation might facilitate and/or stabilise the opening of the flap of the isoenzyme with the highest flap flexibility and hydrophobicity of the catalytic pocket (mLip3).…”

Section: Effect Of the Chemical Nature Of The Interfaces Activation mentioning

confidence: 99%

Regulation of the interfacial activation within the Candida rugosa lipase family

Pernas¹,

Pastrana²,

Fuciños³

et al. 2009

J of Physical Organic Chem

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The fungus Candida rugosa produces several lipase isoenzymes and the 3D structure of three was solved (Lip1, Lip2 and Lip3). In an aqueous solution, the hydrophobic catalytic cavity of these lipases is buried under a flap that blocks the entrance of the substrate. In the hydrolysis of triacetin, the limiting step of the catalytic process was the activation of the enzyme and only the existence of the highly hydrophobic interface provided by hexane was able to shift the equilibrium towards the open conformation. In the case of Lip1, the hexane interface was crucial and once the open conformation was stabilised, Lip1 was as efficient as Lip3 for the hydrolysis of triacetin. Lip2 isoenzyme behaves more similarly to mLip3 reinforcing the higher structural and functional similarity between these isoenzymes. Inhibition experiments carried out under non-kinetic conditions allowed to correlate the higher flexibility of the closed flap and the higher hydrophobicity of the catalytic pocket of mLip3 with the greater facility of this isoenzyme to become activated by interfaces of different chemical nature. Both factors might allow a more intense penetration of mLip3 into the interfaces. In these systems, we observed a unique behaviour of Lip2, enzyme that although in a monomeric state and provide with an analogous flap structure to that of Lip1 or Lip3 underwent a very fast activation even in the absence of supramicellar concentrations of surfactants. We determined that the inhibitor itself forms micelles and hypothesised that they might provide an adequate interface for Lip2 activation.

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Synergistic Effects of Surfactants on Kid Pregastric Lipase Catalyzed Hydrolysis Reactions

Cited by 11 publications

References 19 publications

Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica

Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica

Surfactant-assisted enzymatic extraction of piperine from Piper nigrum L

Regulation of the interfacial activation within the Candida rugosa lipase family

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