Modeling of enzymatic activity of free β-glucosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae: Effects of pH and temperature

Kambiré, Marius Sobamfou; Gnanwa, Jacques Mankambou; Boa, David; Kouadio, Eugène Jean Parfait; Kouamé, Lucien Patrice

doi:10.1016/j.bpc.2021.106611

Cited by 7 publications

(7 citation statements)

References 100 publications

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“…The Jurado model gave an acceptable fit for the three myrosinases (R 2 > 90%), and its parameters suggested that myrosinase has two ionizable groups involved in the catalysis. For BMYR and EMYR, at pH below 3, the catalytic nucleophile is ionized, while ionization of the proton donor occurs above pH 3 [29]. The estimated values of pK 1 were 3.4, 3.1, and 4.1, for BMYR, EMYR, and SMYR, respectively.…”

Section: Effect Of Ph On Myrosinases Kineticsmentioning

confidence: 93%

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Kinetic Study and Modeling of Wild-Type and Recombinant Broccoli Myrosinase Produced in E. coli and S. cerevisiae as a Function of Substrate Concentration, Temperature, and pH

2022

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The myrosinase enzyme hydrolyzes glucosinolates, among which is glucoraphanin, the precursor of the anticancer isothiocyanate sulforaphane (SFN). The main source of glucoraphanin is Brassicaceae; however, its natural concentration is relatively low, limiting the availability of SFN. An option to obtain SFN is its exogenous production, through enzymatic processes and under controlled conditions, allowing complete conversion of glucoraphanin to SFN. We characterized the kinetics of wild-type (BMYR) and recombinant broccoli myrosinases produced in E. coli (EMYR) and S. cerevisiae (SMYR) in terms of the reaction conditions. Kinetics was adjusted using empirical and mechanistic models that describe reaction rate as a function of substrate concentration, temperature, and pH, resulting in R2 values higher than 90%. EMYR kinetics differed significantly from those of BMYR and SMYR probably due to the absence of glycosylations in the enzyme produced in E. coli. BMYR and SMYR were subjected to substrate inhibition but followed different kinetic mechanisms attributed to different glycosylation patterns. EMYR (inactivation Ea = 76.1 kJ/mol) was more thermolabile than BMYR and SMYR. BMYR showed the highest thermostability (inactivation Ea = 52.8 kJ/mol). BMYR and EMYR showed similar behavior regarding pH, with similar pK1 (3.4 and 3.1, respectively) and pK2 (5.4 and 5.0, respectively), but differed considerably from SMYR.

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Section: Effect Of Ph On Myrosinases Kineticsmentioning

confidence: 93%

“…Kambiré et al [29] proposed a mechanistic model to describe the activity dependence of weevil β-glucosidase on pH. The bell shape of activity-pH curves suggests that, in the enzyme molecule, there are two catalytically essential ionizable groups.…”

Section: Ph-dependent Modelsmentioning

confidence: 99%

Kinetic Study and Modeling of Wild-Type and Recombinant Broccoli Myrosinase Produced in E. coli and S. cerevisiae as a Function of Substrate Concentration, Temperature, and pH

2022

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“…In the previous works, equation (15) were used to determine the energies activation and optimum temperatures of hydrolysis of inulin: by endo-inulinase Aspergillus niger [22], by exo-inulinases Aspergillus niger [23] and also parameters olive oil hydrolysis by porcine pancreas lipase [11,24]. Equation (15) were applied to estimated parameters by others researchers [25,26].…”

Section: Theory the Effect Of Temperature On Lipase Activitymentioning

confidence: 99%

“…Based on equation (15), the parameters E d and T opt were determined by a non-linear regression according to the Levenberg-Marquardt procedure [21,[22][23][24][25][26], determining the minimum sum of squared errors defined by equation…”

Section: Theory the Effect Of Temperature On Lipase Activitymentioning

confidence: 99%

The Activation Energies and Optimum Temperatures of Olive Oil Hydrolysis By Lipase Porcine Pancreas

Miłek

2021

Ecological Chemistry and Engineering S

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Lipase activity is a perfect indicator for the monitoring of processes of bioremediation of degraded soils. Lipase is also used in the processes of oil hydrolysis in wastewater treatment. To be able to predict and model processes with used lipase in environmental operations, knowledge of the kinetic parameters of the process are required. The paper presents the determined values of activation energies and optimum temperatures for porcine pancreas lipase. The parameters were estimated based on the literature of the activity curves vs. temperature for hydrolysis of olive oil by lipase. It was noticed that concentration of gum arabic added as an emulsifier during lipase activity measurements influences on the obtained values of determined parameters. A mathematical model describing the effect of temperature on porcine pancreas lipase activity was used. Based on the comparison analysis, the optimum temperature Topt were obtained in the range from 313.30 ±0.56 to 319.62 ±0.96 K, activation energies Ea were from 51 ±10 to 82.6 ±9.9 kJ/mol, and values of deactivation energies Ed were in the range from 122.7 ±4.0 to 150.9 ±5.8 kJ/mol.

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“…R. palmarum can damage the plant in two ways, directly, by the attack of larvae that cause open galleries, destroying the plant's internal apical tissues (Murguía‐González et al, 2018; Santana et al, 2014), or indirectly (through the adults) as vectors of red ring disease (Kambiré et al, 2021) and coconut resinosis (Costa e Carvalho et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Characterization of cultivable intestinal microbiota in Rhynchophorus palmarum Linnaeus (Coleoptera: Curculionidae) and determination of its cellulolytic activity

Calumby

Almeida

Barros

et al. 2022

Arch Insect Biochem Physiol

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Rhynchophorus palmarum Linnaeus is an agricultural pest that affects various palm crops, including coconut (Cocos nucifera) plantations which are prominent in the economy of Northeastern Brazil. Characterization of the intestinal microbiota of R. palmarum, as well as elucidation of aspects related to the biochemistry and physiology of the insect's digestion, is essential for intervention in specific metabolic processes as a form of pest control. Thus, this study aimed to characterize the intestinal microbiota of R. palmarum and investigate its ability to degrade cellulosic substrates, to explore new biological control measures. Intestinal dissection of eight adult R. palmarum insects was performed in a laminar flow chamber, and the intestines were homogenized in sterile phosphate‐buffered saline solution. Subsequently, serial dilution aliquots of these solutions were spread on nutritive agar plates for the isolation of bacteria and fungi. The microorganisms were identified by matrix‐assisted laser desorption/ionization with a time‐of‐flight mass spectrometry and evaluated for their ability to degrade cellulose. Fourteen bacterial genera (Acinetobacter, Alcaligenes, Arthrobacter, Bacillus, Citrobacter, Enterococcus, Kerstersia, Lactococcus, Micrococcus, Proteus, Providencia, Pseudomonas, Serratia, and Staphylococcus) and two fungal genera (Candida and Saccharomyces)—assigned to the Firmicutes, Actinobacteria, Proteobacteria, and Ascomycota phyla—were identified. The cellulolytic activity was exhibited by six bacterial and one fungal species; of these, Bacillus cereus demonstrated the highest enzyme synthesis (enzymatic index = 4.6). This is the first study characterizing the R. palmarum intestinal microbiota, opening new perspectives for the development of strategies for the biological control of this insect.

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Modeling of enzymatic activity of free β-glucosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae: Effects of pH and temperature

Cited by 7 publications

References 100 publications

Kinetic Study and Modeling of Wild-Type and Recombinant Broccoli Myrosinase Produced in E. coli and S. cerevisiae as a Function of Substrate Concentration, Temperature, and pH

Kinetic Study and Modeling of Wild-Type and Recombinant Broccoli Myrosinase Produced in E. coli and S. cerevisiae as a Function of Substrate Concentration, Temperature, and pH

The Activation Energies and Optimum Temperatures of Olive Oil Hydrolysis By Lipase Porcine Pancreas

Characterization of cultivable intestinal microbiota in Rhynchophorus palmarum Linnaeus (Coleoptera: Curculionidae) and determination of its cellulolytic activity

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