Evaluation of temperature and moisture response surface on the lipase from pumpkin seeds fermentation using Aspergillus niger

Santos, Rafaela Cristiane Andrade; Araújo, Kyzzes Barreto; Soares, Cleide Mara Faria; Aquino, Luciana Cristina Lins de

doi:10.4025/actascitechnol.v34i3.12497

Cited by 9 publications

(18 citation statements)

References 26 publications

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“…Free enzyme reached maximum relative activity (100%) at 37°C, decreasing the activity at subsequent temperatures (Figure 2). Kamini et al (1998), Namboordiri and Chattopadhyaya (2000) and Saxena et al (2003), obtained an optimal temperature of 37°C, between 35 and 55°C and between 28 and 30°C respectively for Aspergillus niger, Aspergillus carneus and Aspergillus oryzae lipase.…”

Section: Effect Of Ph and Temperature On The Hydrolytic Activity Of Fmentioning

confidence: 99%

“…The production of lipase was performed according to methodology described by Santos et al (2012). First, the pumpkin seeds were dried in a dryer (Pardal -PE 100, Brazil) at 60°C, for 8h, ground in a Wiley-type mill with an average diameter of 1.06 mm and sterilized in an autoclave at 121°C for 15 min.…”

Section: Solid State Fermentationmentioning

confidence: 99%

“…In an organic medium, they catalyze a number of useful reactions including esterification, transesterification, acidolysis, alcoholysis, regioselective acylation of glycols and menthols, and synthesis of peptides and other chemicals (SHARMA et al, 2001). Lipases are actually versatile catalysts applicable in a wide range of industrial processes, such as textile, paper, detergents, oil chemicals, food and pharmaceutical industries (SAXENA et al, 2003;YANG et al, 2010). Solidstate fermentation (SSF) is frequently used for lipase production and cultivation media with different residues have been reported, e.g.…”

Section: Introductionmentioning

confidence: 99%

“…Solidstate fermentation (SSF) is frequently used for lipase production and cultivation media with different residues have been reported, e.g. by-products from the refining process of corn oil or olive oil (DAMASO et al, 2008) or pumpkin seed flour (SANTOS et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2014

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ABSTRACT. Immobilization potential of lipase from Aspergillus niger on sol-gel matrix was evaluated by physical adsorption and covalent binding and the biochemical characterization of free and immobilized enzyme was performed. Lipase was produced by solid state fermentation of pumpkin seed flour with 30% moisture, at 30°C for 120h. The enzyme was pre-purified with ammonium sulfate and immobilized in the sol-gel matrix by covalent attachment and physical adsorption. A higher yield of immobilization (81.88%) was obtained in the latter. The free enzyme presented higher hydrolytic activity with pH 4.0, at 37°C; moreover, it was more stable with pH between 6.0 and 7.0, at 35°C. The immobilized lipase showed maximum hydrolytic activity with pH 11.0, at 50°C; it was more stable with pH 11.0, at 37°C. Parameters K m and V max were best determined by Hanes-Woolf linearization.Keywords: enzyme, sol-gel, agroindustrial residue.Lipase microbiana obtida pela fermentação de sementes de abóbora: potencial de imobilização em matrizes hidrofóbicas RESUMO. O objetivo deste trabalho foi avaliar o potencial de imobilização da lipase de Aspergillus niger em sílica por adsorção física e ligação covalente, e realizar a caracterização bioquímica da mesma na forma livre e imobilizada. A lipase foi produzida por fermentação em estado sólido da farinha de sementes de abóbora, contendo 30% de umidade, à temperatura de 30°C em 120h. A seguir, a enzima foi pré-purificada com sulfato de amônio e imobilizada em matriz sol-gel por ligação covalente e adsorção física, obtendo-se nesta última maior rendimento de imobilização (81,88%). A enzima livre apresentou maior atividade hidrolítica em pH 4,0 a 37°C, sendo mais estável em valores de pH entre 6,0 e 7,0 e temperatura de 35°C. A lipase imobilizada por adsorção física apresentou máxima atividade hidrolítica em pH 11,0 e temperatura de 50°C sendo mais estável em pH 11,0 e temperatura de 37°C. Os parâmetros K m e V máx foram melhor determinados pela linearização de Hanes-Woolf.Palavras-chave: enzima, sol-gel, resíduo agroindustrial.

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Section: Effect Of Ph and Temperature On The Hydrolytic Activity Of Fmentioning

confidence: 99%

Section: Solid State Fermentationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2014

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“…The moisture around 50% provided strong positive fungal growth. Studies on A. niger for lipase production by Santos et al (2012) show a significant influence of the initial moisture content at temperatures similar to those used in this work.…”

Section: Resultsmentioning

confidence: 78%

LIPASE PRODUCTION BY Aspergillus niger GROWN IN DIFFERENT AGRO-INDUSTRIAL WASTES BY SOLID-STATE FERMENTATION

Costa

Hermann

García-Román

et al. 2017

Braz. J. Chem. Eng.

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-Filamentous fungi can easily degrade agro-industrial wastes in solid-state fermentation processes, synthesizing many important commercial biocompounds, such as lipolytic enzymes. The aim of this study was to evaluate the effect of the composition of the solid culture medium on the production of lipolytic enzymes by the fungus Aspergillus niger. Rice, wheat and soybean bran were mixed to prepare the culture medium, which was supplemented with glucose, glycerol or soybean oil. Four mixture experimental designs were used to find the best medium for enzyme production. According to our results, the highest lipolytic activity values were achieved with a mixture of rice bran and glycerol (19.844 U·g -1 ) or with rice bran only (13.267 U·g -1 ). Thus, the lipolytic enzyme could be produced without any additional carbon source apart from rice bran, although glycerol addition induced a higher production.

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Morphological and physicochemical aspects of microbial lipase obtained from novel agroindustrial waste encapsulated in a sol–gel matrix

Zubiolo

Santos

Figueiredo

et al. 2015

J Therm Anal Calorim

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The lipase from Aspergillus niger, obtained from solid-state fermentation of pumpkin seed flour, was encapsulated in a sol-gel matrix. The silica obtained by the sol-gel technique and lipase encapsulated were characterised with regard to superficial area, pore volume and size by nitrogen adsorption (BJH method), scanning electron microscopy, mass loss upon heating (TG) and differential scanning calorimetry. The immobilised biocatalyst and the sol-gel matrix showed features typical of mesoporous solids. The presence of the enzyme encapsulated in the solgel matrix was confirmed since the total mass loss of the BI at a temperature of 1,000°C was approximately 60 %, while for the free enzyme the mass loss was 95 %. This new lipase obtained from the fermentation of agroindustrial waste, which when encapsulated in sol-gel has physicalchemical and morphological features similar to those of conventional biocatalysts, maybe exploited for future applications in biocatalytic processes.

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Evaluation of temperature and moisture response surface on the lipase from pumpkin seeds fermentation using Aspergillus niger

Cited by 9 publications

References 26 publications

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

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

LIPASE PRODUCTION BY Aspergillus niger GROWN IN DIFFERENT AGRO-INDUSTRIAL WASTES BY SOLID-STATE FERMENTATION

Morphological and physicochemical aspects of microbial lipase obtained from novel agroindustrial waste encapsulated in a sol–gel matrix

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