A thermoactive uropygial esterase from chicken: Purification, characterisation and synthesis of flavour esters

Fendri, Ahmed; Louati, Hanen; Sellami, Mohamed; Gargouri, Héla; Smichi, Nabil; Zarai, Zied; Aissa, Imen; Miled, Nabil; Gargouri, Youssef

doi:10.1016/j.ijbiomac.2012.04.008

Cited by 12 publications

(9 citation statements)

References 33 publications

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“…As shown in Fig. 8a, HaSGNH1 could effectively synthesize butyl acetate from 1-butanol and acetic acid based on a gas chromatogram, which is comparable to other enzymes [42,43]. In addition, HaS-GNH1 showed significant catalytic efficiency for butyl butyrate synthesis (Fig.…”

Section: Synthesis Of Butyl and Oleic Estersmentioning

confidence: 64%

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Yoo

Jeon

et al. 2020

Biotechnol Biofuels

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Background: Biodiesel and flavor compound production using enzymatic transesterification by microbial lipases provides mild reaction conditions and low energy cost compared to the chemical process. SGNH-type lipases are very effective catalysts for enzymatic transesterification due to their high reaction rate, great stability, relatively small size for convenient genetic manipulations, and ease of immobilization. Hence, it is highly important to identify novel SGNH-type lipases with high catalytic efficiencies and good stabilities. Results: A promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from Halocynthiibacter arcticus was catalytically characterized and functionally explored. HaSGNH1 displayed broad substrate specificity that included tert-butyl acetate, glucose pentaacetate, and p-nitrophenyl esters with excellent stability and high efficiency. Important amino acids (N83, M86, R87, F131, and I173F) around the substrate-binding pocket were shown to be responsible for catalytic activity, substrate specificity, and reaction kinetics. Moreover, immobilized HaSGNH1 was used to produce high yields of butyl and oleic esters. Conclusions: This work provides a molecular understanding of substrate specificities, catalytic regulation, immobilization, and industrial applications of a promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from H. arcticus. This is the first analysis on biodiesel and flavor synthesis using a cold-adapted halophilic SGNH-type lipase from a Halocynthiibacter species.

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Section: Synthesis Of Butyl and Oleic Estersmentioning

confidence: 64%

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Yoo

Jeon

et al. 2020

Biotechnol Biofuels

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“…The same behavior was obtained with CUE (75 and 20 mM) (Table ) (Fendri et al . ). The discrepancies observed in the kinetic behavior of esterases and lipases toward short‐chain esters are consistent with the conclusion that the activity of these enzymes depends strongly on the physical state of the substrate.…”

Section: Resultsmentioning

confidence: 97%

A High Salt-Tolerant Thermoactive Esterase from Golden Grey Mullet: Purification, Characterization and Kinetic Properties

Smichi¹,

Fendri²,

Gargouri³

et al. 2015

Journal of Food Biochemistry

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An esterase was purified from the golden grey mullet viscera using successively a Sephacryl S-100 gel filtration, an anion-exchange chromatography and a highperformance liquid chromatography filtration column. The pure esterase (GmDE) is a monomer that has a molecular mass of about 55 kDa, as determined by SDS-PAGE analysis. The purified enzyme displayed a specific activity of 100 U/mg on short-chain triacylglycerols at a temperature of 50C. GmDE is therefore a thermoactive enzyme as compared to other fish lipolytic enzymes that have been studied so far. No significant lipolytic activity was noticed when long-chain triacylglycerol (olive oil) was used as a substrate. It is worth noting that the pure esterase was active in the presence of salt concentrations as high as 0.8 M. The GmDE N-terminal amino acid sequence showed no similarities with that of other known fish esterases. Altogether, these results suggest that the GmDE is a member of a new group of digestive esterases belonging to vertebrates. PRACTICAL APPLICATIONSCharacterization of an esterase from low-value fish viscera and the use of digestive enzyme may add value to this discarded species. Furthermore, the activity and stability at alkaline pH may also find use in laundry detergents. The thermoactivity of the purified esterase makes it a good candidate for potential application in food processing operations. Finally, the stability of the enzyme in high salt concentrations suggests that it can be used as an additive in different processes (food, cosmetic and pharmaceutical operations).

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“…Anhydrous zinc octanoate (Zn(C 7 H 15 COO) 2 ) was synthesized and characterized, and showed promising catalytic activity for the synthesis of isopropyl octanoate, especially at 165 °C, isopropanol:octanoic acid molar ratios of 8:1 and 6:1, and with 7 and 10% catalyst. The results corresponding to the center point from the experiment should also be noted, because they presented significant conversion gains.…”

Section: Resultsmentioning

confidence: 99%

“…[1][2][3][4] Among such esters, isopropyl octanoate, derived from the process of isopropanol esterification with octanoic acid in the presence of an acid catalyst (typically sulfuric or hydrochloric acid) in homogeneous medium, requires a complex process to remove the products and neutralize the acid catalyst. 5 Other solid acid catalysts have also been reported, but due to high acidity, parallel reactions are frequently observed.…”

Section: Introductionmentioning

confidence: 99%

Isopropyl Octanoate Synthesis Catalyzed by Layered Zinc n-Octanoate

Maruyama¹,

Kanda²

2016

J. Braz. Chem. Soc.

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Isopropyl octanoate is an ester used in the formulation of cosmetics, foods, medicines, and other products. The peculiar thermodynamic and kinetic factors, allied with the demand for the applications mentioned above, justify the development of an optimized process for its synthesis. In the present article, the esterification of octanoic acid with isopropanol while using zinc n-octanoate as catalyst is reported. A factorial design was employed where variables such as molar ratio (alcohol:acid), percentage of catalyst (in relation to the acid mass) and temperature were investigated. It was observed that zinc octanoate showed promising catalytic activity, especially at 165 °C, with molar ratios of 8:1 and 6:1, and with 7 and 10% of catalyst, where conversions up to 75% were observed. Optimized conditions for the production of isopropyl octanoate were determined to be 165 °C, 6:1 molar ratio and 5.97% of catalyst.

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A thermoactive uropygial esterase from chicken: Purification, characterisation and synthesis of flavour esters

Cited by 12 publications

References 33 publications

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

A High Salt-Tolerant Thermoactive Esterase from Golden Grey Mullet: Purification, Characterization and Kinetic Properties

Isopropyl Octanoate Synthesis Catalyzed by Layered Zinc n-Octanoate

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