Optimisation, purification and characterisation of extracellular lipase from Botryococcus sudeticus (UTEX 2629)

Yong, Suh Kuan; Lim, Boon Hoe; Saleh, Said; Tey, Lai-Hock

doi:10.1016/j.molcatb.2016.02.004

Cited by 25 publications

(5 citation statements)

References 35 publications

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“…Microbial lipases as being more stable than animal or plant lipases, have earned special industrial attention due to their stability, selectivity and broad substrate specificity. Lipases have different applications: chemical, detergents, textile, pharmaceutical, cosmetic, paper, agrochemical, olechemical, dairy and food industries, synthesis of biosurfactant and production of biodiesel (Rathi et al 2002;Sharma et al 2002Sharma et al , 2014Kumar et al 2011;Rajendran and Thangavelu 2012;Vasiee et al 2016;Yong et al 2016;Ismail et al 2017). Microbial lipase has different biocatalytic activities in aqueous and nonaqueous systems, such as hydrolysis, interesterification, esterification, transesterification, alcoholysis, acidolysis and aminolysis reactions Thangavelu 2007, 2012;Saranya et al 2014;Vasiee et al 2016).…”

Section: Introductionmentioning

confidence: 99%

“…Among the industrial enzymes, lipases are considered worldwide as the third largest total sales volume after protease and carbohydrases (Dahiya and Purkayastha 2011). Moreover, lipases have a great commercial interest as they do not require cofactors and they are active in organic interfaces and versatility work on different substrates (Yong et al 2016). Lipase-producing micro-organisms, including Actinomycetes, bacteria, filamentous fungi and yeasts, can be found in diverse habitats such as industrial wastes, vegetable oil processing factories, dairies, soil contaminated with oil, oilseeds and decaying food (Vasiee et al 2016).…”

Section: Introductionmentioning

confidence: 99%

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Statistical enhancement of lipase extracellular production byBacillus stratosphericusPSP8 in a batch submerged fermentation process

et al. 2018

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Statistical enhancement of lipase extracellular production byBacillus stratosphericusPSP8 in a batch submerged fermentation process

et al. 2018

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“…The partially purified enzyme was pre-incubated with the particular salt solution at 25°C for 1 h and the enzymatic activity was determined afterward [27] (Section 2.9). A pre-incubation temperature of 25°C was used as it was considered suitable to preserve esterase stability [28][29][30]. Additionally, the effect of different solvents (dimethyl sulfoxide (DMSO), dimethylformamide (DMF), methanol, ethanol, n-propanol, butanol, toluene, xylene, n-hexane and isooctane) was also studied.…”

Section: Effects Of Salts and Solvents On Esterase Activitymentioning

confidence: 99%

“…Additionally, the effect of different solvents (dimethyl sulfoxide (DMSO), dimethylformamide (DMF), methanol, ethanol, n-propanol, butanol, toluene, xylene, n-hexane and isooctane) was also studied. The partially purified enzyme was diluted in the organic solvents at a concentration of 50% (v/v) in the reaction mixtures and further pre-incubated for 1 h at 25°C [28][29][30]. After incubation, the enzymatic activity was determined (Section 2.9).…”

Section: Effects Of Salts and Solvents On Esterase Activitymentioning

confidence: 99%

Integrated strategy for purification of esterase from Aureobasidium pullulans

Lemes

Silvério

Rodrigues

et al. 2019

Separation and Purification Technology

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Esterases catalyze the cleavage and formation of ester bonds of a broad range of substrates presenting a widespread spectrum of industrial applications. This work aimed to partially purify and characterize an esterase from Aureobasidium pullulans LABIOTEC 01 produced in a culture medium containing olive mill wastewater. Esterase purification was evaluated using different strategies, namely the enzyme recovery by PEG-salt aqueous twophase systems (ATPSs); and the enzyme precipitation with ammonium sulfate, acetone, and ethanol. The best purification factor (18 ± 2) was obtained when the ATPS composed of 20% (w/w) polyethylene glycol (PEG) 6000 and 5.8% (w/w) potassium phosphate buffer (PPB) pH 8.0 was combined with acetone precipitation. The partially purified enzyme presented an optimum pH of 5.0, although it remained active in the pH range of 4.5 to 7.5 (≥ 50% relative activity). The optimum temperature was found to be 60°C. Furthermore, the addition of salts such as FeCl 3 , CuSO 4 and MnCl 2 promoted an increase in the enzymatic activity (above 100%). The enzyme was found to be stable and showed high activity when exposed to polar solvents such as dimethyl sulfoxide, dimethylformamide, and methanol. The use of an integrated strategy of purification combining simple purification methods such as ATPS and precipitation was herein reported for the first time for esterase. This strategy proved to be an interesting approach to partially purify the esterase produced under submerged fermentation by A. pullulans. Furthermore, the enzyme showed potential to be applied in industrial biocatalytic processes using high temperature and different salts or solvents. Also, the production of esterase using olive mill wastewater as substrate demonstrated to be a suitable alternative to reduce and valorize agro-industrial residues.

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“…The result was a 5.52-fold purification of the extracellular lipase, with a specific activity of 68.055 U/mg. Yong et al [110] studied an extracellular lipase from…”

Section: Chromatographymentioning

confidence: 99%

Produção, caracterização bioquímica e purificação de lipases de Metschnikowia sp. prospectadas do ambiente Antártico utilizando sistema bifásico aquoso

Melani¹,

Natalia²

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Studies of planet's natural resources have been shown as the path to the advancement of technological processes and to the detriment of chemical methods. Thus, the need to search for enzymes with special characteristics that make their application in the industrial field, together with the capacity of survival and adaptation of beings in habitats extreme environments, such as the Antarctic continent, make these microorganisms targets of great biotechnological interest. Specifically, the extraction of lipases from psychrophilic and psychrotolerant fungi has attracted attention due to its high activity at low temperatures, which confers a peculiar property. Alternative technologies are gradually surfacing in the purification of lipases, where aqueous two-phase systems (ATPS) are prominent. In this work, lipases of Mestschnikowia australis CRM 1589., isolated from Antarctic environment, produced under submerged fermentation, were purified and characterized. The enzyme was efficiently extracted with an aqueous two-phase system composed by PEG / sodium phosphate and PEG / ammonium sulfate, with a tendency to phase partition in PEG rich. In addition, the first system has better partitioning results and the second onde showed higher purification factors. The main studies indicated that lipase has alkaline characteristics, stability in a wide range of temperature and low inhibition values to metallic ions. These characteristics confer potential industrial applications for this lipase.

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Optimisation, purification and characterisation of extracellular lipase from Botryococcus sudeticus (UTEX 2629)

Cited by 25 publications

References 35 publications

Statistical enhancement of lipase extracellular production byBacillus stratosphericusPSP8 in a batch submerged fermentation process

Statistical enhancement of lipase extracellular production byBacillus stratosphericusPSP8 in a batch submerged fermentation process

Integrated strategy for purification of esterase from Aureobasidium pullulans

Produção, caracterização bioquímica e purificação de lipases de Metschnikowia sp. prospectadas do ambiente Antártico utilizando sistema bifásico aquoso

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