Immobilization of <i>Aspergillus niger</i><scp>ATCC</scp> 1015 on bionatural structures for lipase production

Osho, Michael Bamitale; ., T.O.S. Popoola; Kareem, Sarafadeen Olateju

doi:10.1002/elsc.201300129

Cited by 6 publications

(7 citation statements)

References 19 publications

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“…The optimum temperature of the free lipase was about 45°C, whereas that of the immobilized enzyme was increased to 55°C ( Figure 3 ). Osho et al [ 12 ] reported in their study on the effect of reaction temperature on lipase activity using structural fibrous network of papaya and vegetable sponge-immobilized lipases of A. niger ATCC 1015 recorded optimum temperature of 45°C for both matrices and ascribed the reason to a consequence of enhanced thermal stability. In support of this finding, Allenza et al [ 26 ] and Kitano et al [ 27 ] reported that the activation energy of the immobilized enzyme was lower than that of the free enzyme (i.e., the higher the temperature, the lower the activation energy), because the internal diffusion of the substrate into the carrier-enzyme system was the rate-limiting the process.…”

Section: Resultsmentioning

confidence: 99%

“…This includes agarose beads, alginate beads [ 3 ], chitosan beads [ 9 ], k-carrageenan beads [ 10 ], and nanogel beads [ 11 ]. Osho et al [ 12 ] have reported the use of bionatural matrices—structural fibrous network (SFN) and vegetable sponge (VS)—for their ability to entrap or immobilize lipase and the effects of immobilization on the temperature, pH, operational stability, and reusability of the lipase were investigated. In the present study, Aspergillus niger F7-02 lipase was immobilized by entrapment in polysaccharide hydrogel beads of Irvingia gabonensis matrix at optimized immobilization conditions for biotechnological industrial application.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization ofAspergillus nigerF7-02 Lipase in Polysaccharide Hydrogel Beads ofIrvingia gabonensisMatrix

2014

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The potential of polysaccharide Irvingia gabonensis matrix as enzyme immobilization support was investigated. Lipase of Aspergillus niger F7-02 was immobilized by entrapment using glutaraldehyde as the cross-linking agent and stabilized in ethanolic-formaldehyde solution. The pH and temperature stability and activity yield of the immobilized enzyme were determined. Such parameters as enzyme load, bead size, number of beads, and bead reusability were also optimized. Adequate gel strength to form stabilized beads was achieved at 15.52% (w/v) Irvingia gabonensis powder, 15% (v/v) partially purified lipase, 2.5% (v/v) glutaraldehyde, and 3 : 1 (v/v) ethanolic-formaldehyde solution. There was 3.93-fold purification when the crude enzyme was partially purified in two-step purification using Imarsil and activated charcoal. Optimum lipase activity 75.3 Ug−1 was achieved in 50 mL test solution containing 15 beads of 7 mm bead size. Relative activity 80% was retained at eight repeated cycles. The immobilization process gave activity yield of 59.1% with specific activity of 12.3 Umg−1 and stabilized at optimum pH 4.5 and temperature 55°C. Thus the effectiveness and cost-efficiency of I. gabonensis as a polymer matrix for lipase immobilization have been established.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization ofAspergillus nigerF7-02 Lipase in Polysaccharide Hydrogel Beads ofIrvingia gabonensisMatrix

2014

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“…The authors showed that the immobilization of lipase successfully enhanced its pH stability, especially in slightly acidic environments. A relative activity above 75 % was achieved for the immobilized lipase stored at 4 C and 50 % at 28 C until the fourth week of storage for both supports [81].…”

Section: Obtainment and Properties Of Lipases From Aspergillusmentioning

confidence: 95%

“…The positive influence of the immobilization process was observed on the thermal stability of the enzyme, since a longer half-life t 1/2 and lower deactivation constant were obtained with the encapsulated lipase when compared with the free lipase [80]. Osho et al [81] tested the lipase immobilization produced by A. niger ATCC 1015 in matrices of a structural fibrous network of pawpaw (Carica papaya) wood and vegetable sponge (Luffa aegyptiaca) by entrapment. The authors showed that the immobilization of lipase successfully enhanced its pH stability, especially in slightly acidic environments.…”

Section: Obtainment and Properties Of Lipases From Aspergillusmentioning

confidence: 99%

Aspergillus Lipases: Biotechnological and Industrial Application

Contesini¹,

Calzado²,

Madeira³

et al. 2016

Fungal Metabolites

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Lipases are enzymes with remarkable properties and catalytic versatility. These proteins are capable of catalyzing hydrolytic and synthetic reactions, allowing the production of different compounds. Aspergillus are important producers of lipases, since they are able to secrete large amounts of these proteins to the extracellular media. Several studies have reported the importance of fermentation parameters as well as genetic engineering of Aspergillus strains in order to improve lipase production. Different Aspergillus species secrete lipases with interesting characteristics such as thermostability, stability in a wide pH range, stability in organic solvents, and enantioselectivity toward the substrate. The obtainment of lipases with highlighted characteristics for use in industry is the main focus of several studies. Such lipases can be obtained with screening of Aspergillus strains, protein engineering, and immobilization of lipases that can frequently improve thermostability and enantioselectivity. Among the applications of lipases from Aspergillus, there are studies on the improvement of sensorial properties of different products in the food industry, compatibility with detergents for removal of fat stains from fabrics, and the obtainment of enantiopure pharmaceuticals.

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“…Additionally, papaya trunk wood is very cheap and abundantly available. Several microorganisms have been immobilized in papaya trunk wood, i.e., Aspergillus niger (Osho et al, 2014), Aspergillus tamarii (Maduka et al,Halim et al / JIPK,13(2):208-221…”

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Immobilization of Providencia stuartii Cells in Papaya Trunk Wood for N-acetylglucosamine Production from Pennaeus vannamei Shrimp Shells

Halim

Tantradjaja

Hardoko

et al. 2021

JIPK

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Highlight Research AbstractChitin is a natural compound found abundantly in shrimp shells. Chitin can be degraded to produce N-acetylglucosamine, which has wide applications in the food and pharmaceutical fields. Fermentation using chitinolytic microorganisms can be used to produce N-acetylglucosamine from shrimp shells’ chitin. One of the strong chitinolytic bacteria that was isolated from previous research was Providencia stuartii. To provide better stability and efficiency in fermentation, P. stuartii cells were immobilized using entrapment method in papaya trunk wood. The aims of this research were to determine the optimum papaya trunk wood size, ratio of papaya trunk wood and growth medium, as well as the optimum fermentation cycle to produce N-acetylglucosamine from P. vannamei shrimp shells using submerged fermentation method. The research used experimental method with treatment of different sizes of papaya trunk wood (1 x 1 x 1 cm3, 1.5 x 1.5 x 1.5 cm3, and 2 x 2 x 2 cm3), different ratio of papaya trunk wood and growth medium (1:10, 1:15 and 1:20), and 4 fermentation cycles. Results showed that papaya trunk wood with size of 1 x 1 x 1 cm3 and ratio (w/v) of 1:10 could immobilize 87.08±2.05% of P. stuartii cells and produce the highest N-acetylglucosamine concentration, which was 238177.78±3153.48 ppm. The highest N-acetylglucosamine production was obtained from first fermentation cycle and decreased over the last three cycles, but still produced high concentration of N-acetylglucosamine. Therefore, it is possible to perform continuous N-acetylglucosamine production from shrimp shells using P. stuartii cells immobilized in papaya trunk wood.

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Immobilization of Aspergillus nigerATCC 1015 on bionatural structures for lipase production

Cited by 6 publications

References 19 publications

Immobilization ofAspergillus nigerF7-02 Lipase in Polysaccharide Hydrogel Beads ofIrvingia gabonensisMatrix

Immobilization ofAspergillus nigerF7-02 Lipase in Polysaccharide Hydrogel Beads ofIrvingia gabonensisMatrix

Aspergillus Lipases: Biotechnological and Industrial Application

Immobilization of Providencia stuartii Cells in Papaya Trunk Wood for N-acetylglucosamine Production from Pennaeus vannamei Shrimp Shells

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