&lt;b&gt;Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices&lt;b&gt;

Santos, Rafaela Cristiane Andrade; Araújo, Kyzzes Barreto; Zubiolo, Claudia; Soares, Cleide Mara Faria; Lima, Álvaro Silva; Aquino, Luciana Cristina Lins de

doi:10.4025/actascitechnol.v36i2.18275

Cited by 14 publications

(8 citation statements)

References 34 publications

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“…This result was close to that obtained by Santos et al (2017), who immobilised A. niger lipase obtained from H. speciosa seeds on a sol-gel matrix by covalent bonding with an immobilisation yield of 91.6%. However, these results were higher than those obtained by Santos et al (2014), where the A. niger lipase obtained from pumpkin seeds was immobilised on a sol-gel matrix by covalent bonding (immobilisation yield 81.9%) and physical adsorption (immobilisation yield 58.2%).…”

Section: Immobilisation Of Lipase On Pes Membranescontrasting

confidence: 56%

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Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

et al. 2019

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In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.

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Section: Immobilisation Of Lipase On Pes Membranescontrasting

confidence: 56%

“…The enzyme immobilisation by physical adsorption was performed according to Santos et al (2014). A mixture that contained 1 mL of enzymatic solution (300 mg mL -1 ) in sodium acetate buffer (0.2 M, pH 4.0), 9 mL of hexane, and 1 g of PES membrane was prepared and stirred for 3h.…”

Section: Enzyme Immobilisation On Pes Membranes By Physical Adsorptiomentioning

confidence: 99%

Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

et al. 2019

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“…Pumpkin seeds could be used as a valuable, economical and abundant source to produce natural enzymes such as lipase. Recently, lipase from Cucurbita moschata was purified using gel filtration chromatography [17]. In another study pumpkin seed oil lipase was extracted using supercritical fluid extraction [18].…”

Section: Introductionmentioning

confidence: 99%

A Novel Aqueous Two Phase System Composed of Surfactant and Xylitol for the Purification of Lipase from Pumpkin (Cucurbita moschata) Seeds and Recycling of Phase Components

et al. 2015

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Lipase is one of the more important enzymes used in various industries such as the food, detergent, pharmaceutical, textile, and pulp and paper sectors. A novel aqueous two-phase system composed of surfactant and xylitol was employed for the first time to purify lipase from Cucurbita moschata. The influence of different parameters such as type and concentration of surfactants, and the composition of the surfactant/xylitol mixtures on the partitioning behavior and recovery of lipase was investigated. Moreover, the effect of system pH and crude load on the degree of purification and yield of the purified lipase were studied. The results indicated that the lipase was partitioned into the top surfactant rich phase while the impurities partitioned into the bottom xylitol-rich phase using an aqueous two phase system composed of 24% (w/w) Triton X-100 and 20% (w/w) xylitol, at 56.2% of tie line length (TLL), (TTL is one of the important parameters in this study and it is determined from a bimodal curve in which the tie-line connects two nodes on the bimodal, that represent concentration of phase components in the top and bottom phases) and a crude load of 25% (w/w) at pH 8.0. Recovery and recycling of components was also measured in each successive step process. The enzyme was successfully recovered by the proposed method with a high OPEN ACCESSMolecules 2015, 20 11185 purification factor of 16.4 and yield of 97.4% while over 97% of the phase components were also recovered and recycled. This study demonstrated that the proposed novel aqueous two phase system method is more efficient and economical than the traditional aqueous two phase system method for the purification and recovery of the valuable enzyme lipase.

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“…Technology Maringá, v. 39, n. 1, p. 1-8, Jan.-Mar., 2017 Mussatto, 2009;Pandey, Soccol, & Mitchell, 2000;Salihu et al, 2012;Santos et al, 2014). These enzymes are important due to their versatility in industrial applications since they catalyze a variety of reactions, such as partial or complete hydrolysis of triacylglycerols and the esterification, transesterification and interesterification of lipids (Colla et al, 2010;Salihu et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

<b>Lipase from <i>Aspergillus niger</i> obtained from mangaba residue fermentation: biochemical characterization of free and immobilized enzymes on a sol-gel matrix

et al. 2017

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ABSTRACT. In this study, mangaba residue (seeds) was used as a substrate for Aspergillus niger lipase production by solid-state fermentation. The partially purified enzyme was efficiently immobilized in a sol-gel matrix by covalent bonding with an immobilization yield of 91.2%. The immobilized biocatalyst and free lipase had an optimum pH of 2.0 and 5.0, respectively. However, greater stability was obtained at pH 4.0 and 7.0, respectively. The biocatalysts showed stability at the optimum temperature of 55°C, where the residual activity was above 87% after 240 min., of incubation. The lower deactivation constant (k d ) and higher half-life of the immobilized biocatalyst indicated greater thermal stability than those obtained with the free enzyme. The Michaelis Constant (K m ) (77 and 115 mM for free and immobilized lipase, respectively) and maximum reaction rate (V max ) (1250 and 714 U mg -1 for free and immobilized lipase, respectively) indicated that the immobilization process reduced enzyme-substrate affinity. Regarding the operational stability, the biocatalyst showed relative activity above 50% until seven cycles of reuse in olive oil hydrolysis. This novel biocatalyst obtained from a tropical fruit residue showed biochemical characteristics that support its application in future biocatalysis studies.Keywords: fruit residue, sol-gel, biotechnology, enzyme.Lipase de Aspergillus niger obtida a partir da fermentação do resíduo de mangaba: caracterização bioquímica das enzimas livre e imobilizada em matriz de sol-gel RESUMO. Neste estudo, o resíduo de mangaba (sementes) foi utilizado como substrato para a produção de lipase de Aspergillus niger por fermentação em estado sólido. A enzima parcialmente purificada foi eficientemente imobilizada em matriz de sol-gel por ligação covalente visto que o rendimento de imobilização foi de 91,2%. O biocatalisador imobilizado e a lipase livre mostraram pH ótimo de 2,0 e 5,0, respectivamente. Entretanto, a maior estabilidade foi obtida nos pHs 4,0 e 7,0, respectivamente. Os biocatalisadores mostraram estabilidade na temperatura ótima de 55°C em que a atividade residual foi superior a 87% após 240 min., de incubação. A menor constante de desativação (k d ) e o maior tempo de meia-vida do biocatalisador imobilizados demonstraram maior estabilidade térmica do que a obtida pela enzima livre. Os parâmetros constantes de Michaelis (K m ) (77 e 115 mm, para as enzimas livre e imobilizada, respectivamente) e velocidade máxima de reação (V máx ) (1250 e 714 U mg -1 , para as enzimas livre e imobilizada, respectivamente) indicaram que o processo de imobilização reduziu a afinidade enzima-substrato. Em relação à estabilidade operacional, o biocatalisador demonstrou atividade relativa acima de 50% até sete ciclos de reutilização na hidrólise do azeite. Este novo biocatalisador, obtido a partir de um resíduo de fruta tropical, apresentou características bioquímicas que justificam sua aplicação em estudos futuros de biocatálise.Palavras-chave: resíduo de fruta, sol-gel, biotecnologia, enz...

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<b>Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices<b>

Cited by 14 publications

References 34 publications

Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

A Novel Aqueous Two Phase System Composed of Surfactant and Xylitol for the Purification of Lipase from Pumpkin (Cucurbita moschata) Seeds and Recycling of Phase Components

<b>Lipase from <i>Aspergillus niger</i> obtained from mangaba residue fermentation: biochemical characterization of free and immobilized enzymes on a sol-gel matrix

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