Immobilization studies and biochemical properties of free and immobilized Rhizopus oryzae lipase onto CaCO3: A comparative study

Ghamgui, Hanen; Miled, Nabil; Karra-Châabouni, Maha; Gargouri, Youssef

doi:10.1016/j.bej.2007.03.006

Cited by 54 publications

(36 citation statements)

References 27 publications

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“…Usually, enzymes display an enhancement of stability after being immobilized, 28,43,44 so the effect of temperature and pH on the stability of nROL and rROL was studied in solution as well as immobilized on EP100 and Eupergit V R C. The optimum values of pH and temperature for the stability do not have to coincide with the optimum values of activity; therefore, the operation conditions selected must be a compromise between both variables. Figure 4 summarizes the experimental design.…”

Section: Stabilitymentioning

confidence: 99%

“…[28][29][30][31] Native extract containing R. oryzae lipase (nROL) and an extract containing the recombinant lipase (rROL) have been characterized in a previous study in our laboratory. 32 Although the molecular weight of pure native ROL is cited 33 three forms of lipase in nROL were found with a predominant band of a molecular weight higher than 34 kDa.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

Guillén

Benaiges

Valero

2011

Biotechnology Progress

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The stability of a soluble extract containing a recombinant lipase from Rhizopus oryzae (Cursive) lipase (rROL) produced by Pichia pastoris (Cursive), as well as that for the commercial extract containing the lipase produced by the native organism (nROL), was investigated. The results showed higher residual activity values of the commercial protein compared with the recombinant one. Moreover, two different kinds of support, the polypropylene powder EP100 and Eupergit®C, were tested to immobilize the enzymes. The residual activity of the immobilizated derivatives was also tested to determine whether their stability was enhanced. The results showed a slight improvement in rROL using both supports but a decrease in nROL using Eupergit®C. The study of the residual activity of soluble and immobilized enzymes was performed by means of a central composite rotatable experiment design. In addition, EP100 adsorption isotherms were determined.

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Section: Stabilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

Guillén

Benaiges

Valero

2011

Biotechnology Progress

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“…Moreover, there is the possibility of lipase in an open form and capable of showing improved activity in immobilized condition [148]. Different techniques for immobilization of lipases, such as physical adsorption, covalent bonding to a solid support [149], and physical entrapment within a polymer matrix support [150] have been used to protect the lipase from the nonpolar solvent environment and enable its reuse. Among the immobilization techniques, the adsorption is one of the simplest methods with a higher commercial potential than other methods.…”

Section: Immobilization Of Lipasesmentioning

confidence: 99%

Overview of Fungal Lipase: A Review

Singh

Mukhopadhyay

2011

Appl Biochem Biotechnol

341

200

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Lipases (triacylglycerolacyl hydrolases, EC3.1.1.3) are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. In this review paper, an overview regarding the fungal lipase production, purification, and application is discussed. The review describes various industrial applications of lipase in pulp and paper, food, detergent, and textile industries. Some important lipase-producing fungal genera include Aspergillus, Penicillium, Rhizopus, Candida, etc. Current fermentation process techniques such as batch, fed-batch, and continuous mode of lipase production in submerged and solid-state fermentations are discussed in details. The purification of lipase by hydrophobic interaction chromatography is also discussed. The development of mathematical models applied to lipase production is discussed with special emphasis on lipase engineering.

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“…This fact is important since the biocatalyst produced by SSF was air-dried without any additional treatment to improve its stability. In contrast, the lipase produced by Rhizopus oryzae maintained near to 100% of its activity after 235 days of storage once that it was extracted and immobilized on CaCO 3 [31].…”

Section: Biocatalyst Stabilitymentioning

confidence: 81%

Organic Phase Synthesis of Ethyl Oleate Using Lipases Produced by Solid-state Fermentation

Martı́nez-Ruiz

Garcı́a

Saucedo‐Castañeda

et al. 2008

Appl Biochem Biotechnol

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This paper reports a study of the enzymatic esterification of oleic acid and ethanol. The reaction was catalyzed by lipases produced by solid-state fermentation with Rhizopus sp. Olive oil and perlite were used as an inducer and inert support, respectively. Synthesis of ethyl oleate was carried out in a 10-mL batch reactor with magnetic stirring. The effects of substrate ratios, biocatalyst concentration, and temperature on the reaction rate and conversion efficiency were evaluated. The highest reaction rate (1.64 mmol/L min) was reached with an oleic acid/ethanol mol ratio of 1:5 (oleic acid 50 mM:ethanol 250 mM) and 1 g of biocatalyst. Conversions approaching 100% were obtained after 60 min of reaction at 45 degrees C with n-hexane as a solvent. The initial reaction rate increased proportionally with respect to biocatalyst concentration, which suggests that the reaction rate was not controlled by mass transfer. The biocatalyst retained more than 80% of its catalytic activity after 7 months of storage at 4 degrees C. The results demonstrate that the biocatalyst produced by Rhizopus sp. in solid-state fermentation can be successfully used for ethyl oleate synthesis over short reaction periods under conditions when ethanol is in excess.

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Immobilization studies and biochemical properties of free and immobilized Rhizopus oryzae lipase onto CaCO3: A comparative study

Cited by 54 publications

References 27 publications

Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants

Overview of Fungal Lipase: A Review

Organic Phase Synthesis of Ethyl Oleate Using Lipases Produced by Solid-state Fermentation

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