Assessment of pectinase production by Aspergillus oryzae in growth-limiting liquid medium under limited and non-limited oxygen supply

Meneghel, Lenara; Reis, Guilherme Pellenz; Reginatto, Caroline; Malvessi, Eloane; Silveira, Maurício Moura da

doi:10.1016/j.procbio.2014.07.021

Cited by 29 publications

(17 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Aspergillus oryzae is a filamentous fungus extensively used in the production of beverages and traditional foods in Asia, such as the sake, soy sauce, and soybean paste [1]. This fungus is equipped with a variety of high-value industrial enzymes such as α-amylase, pectinase, and β-galactosidase, involving in the hydrolysis and synthesis of metabolites which enhances the flavor and nutrition of fermented food [2,3]. Moreover, this fungus is considered as a suitable host for heterologous protein production and thus used for producing commercial enzymes [1].…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae

Zhang

Hú

et al. 2019

Braz J Microbiol

View full text Add to dashboard Cite

Oxysterol-binding proteins (OSBPs) comprise a family of sterol-binding proteins. In this study, we focused on AoOSBP1, one of the five OSBP proteins identified from the industrial fungus Aspergillus oryzae. The temporal expression pattern analysis showed that the expression of AoOSBP1, in both gene and protein levels, was stably expressed throughout the developmental stages, while was upregulated during the accelerated growth stage. The immunofluorescence observation revealed that AoOSBP1 protein was mainly distributed in the conidiophore, indicating its underlying role in spore formation. The ligand-binding domain of AoOSBP1, namely OSBP-related domain (ORD), was heterologously expressed in Escherichia coli and purified. The binding assay carried out using microscale thermophoresis showed that the recombinant AoORD protein exhibited binding affinity for ergosterol, and exhibited much higher affinity to oxysterols (25-hydroxycholesterol and 7-ketocholesterol) and phytosterols (βsitosterol and stigmasterol). By contrast, MBP tag as the negative control showed no binding affinity for sterols. The present work demonstrates that AoORD domain in AoOSBP1 is capable of binding sterols, plays an underlying role in sterols transportation, and may participate in spore formation.

show abstract

Section: Introductionmentioning

confidence: 99%

Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae

Zhang

Hú

et al. 2019

Braz J Microbiol

View full text Add to dashboard Cite

show abstract

“…Pectinase activity was evaluated by the method described by Meneghel et al [14]. Hemicellulase activity was analyzed by xylanase activity measured according to Diogo et al's method [15].…”

Section: Enzyme Assaysmentioning

confidence: 99%

Enzyme-Assisted Extraction of Oil from Wet Microalgae Scenedesmus sp. G4

et al. 2015

View full text Add to dashboard Cite

Abstract:The enzyme-assisted aqueous extraction of oil from wet microalgae was employed to avoid the energy consumption of a dewatering process. In this paper, oil-rich microalgae Scenedesmus sp. G4 was hydrolyzed by enzyme mixtures for oil extraction. The results showed that the algae concentration had the greatest influence on yield of extracted oil, and the temperature and the ratio of enzyme mixtures affected the results as follows: the maximum yield of oil extracted from Scenedesmus sp. G4 reached 86.1% under optimal conditions with an algae concentration at 2.5 g/L, temperature 30/50 °C, pH 3.5/4.5 and a cellulase:pectinase:hemicellulase ratio of 1:1:1 or 1:2:1 (w/w/w). The results also indicated that the enzyme mixtures had a significant impact on the integrity of microalgae cells and the crystallization index increased from 30.7% to around 36.0% after enzymatic hydrolysis treatment. The cell wall of Scenedesmus sp. G4 has a high content of cellulose Iα and low crystallization, which is beneficial to the oil extraction by the enzyme-assisted hydrolysis method.

show abstract

“…O extrato pectinolítico testado foi obtido em cultivo submerso de A. oryzae IPT -301 em meio contendo extrato de farelo de trigo, glicose, pectina cítrica (gentilmente cedida pela CPKelco, Brasil), extrato de levedura e sais (Meneghel et al, 2014). Os cultivos foram conduzidos em biorreator BioFlo/CelliGen 115 (New Brunswick), com 4 L de meio a 28 ºC, por 144 h.…”

Section: Materiais E Métodosunclassified

CARACTERIZAÇÃO DE EXTRATO PECTINOLÍTICO PRODUZIDO POR Aspergillus oryzae IPT-301

Rossi

Pozza²,

Negri³

et al. 2015

Anais Do Congresso Brasileiro De Engenharia Química Em Iniciação Científica - Cobeq IC 2015

View full text Add to dashboard Cite

RESUMO -Pectinases são enzimas hidrolíticas largamente utilizadas na indústria, especialmente na produção de vinhos e sucos de frutas. A ação das pectinases obtidas com fungos filamentosos, como Aspergillus oryzae, é fortemente influenciada por parâmetros como a concentração de substrato, o pH e a temperatura. Os três parâmetros interferem na velocidade de reação, enquanto os dois últimos atuam diretamente sobre a estabilidade do complexo. O objetivo deste trabalho foi caracterizar um extrato pectinolítico produzido por A. oryzae IPT-301 em processo submerso, com respeito à temperatura, ao pH e à concentração de substrato, avaliar a sua termoestabilidade e determinar as suas constantes cinéticas. A atividade total de pectinases (TPA) apresentou aumento gradativo a partir de pH 2,5 e foi máxima em 4,0. Para as temperaturas testadas, houve incremento da TPA até 50 ºC, chegando à redução de cerca de 90 % da atividade a 60 °C. Após 150 minutos a 50 ºC, cerca de 37 % da TPA inicial foi mantida e obteve-se t 1/2 de 108 minutos. A cinética enzimática se ajustou ao modelo de Michaelis-Menten (R 2 = 0,927) e os valores de K m = 0,93 mg/mL e V m = 31,6 U/mL foram determinados. O baixo valor de K m , inferior ao encontrado na literatura (1,42 mg/mL), indica a alta afinidade da enzima ao substrato. As pectinases produzidas possuem características semelhantes às das preparações comerciais, sugerindo a possibilidade de seu uso no desenvolvimento de formulações enzimáticas para a indústria. INTRODUÇÃOO uso de enzimas vem ganhando espaço em processos industriais, principalmente no ramo alimentício, uma vez que são catalisadores altamente específicos para seus substratos. Quando comparadas aos catalisadores químicos, as enzimas contribuem para processos capazes de gerar produtos de qualidade por tecnologias limpas. Ainda assim, apenas uma pequena variedade de enzimas é utilizada em grande escala na indústria de alimentos, incluindo-se neste grupo as pectinases, enzimas de uso consagrado nesse setor (Bon, et al., 2008). As enzimas pectinolíticas são capazes de degradar substâncias pécticas que conferem alta viscosidade e turbidez a sucos de frutas e vinhos, facilitando as etapas de filtração e concentração e aumentando o rendimento global do processo. As pectinases também são aplicadas em outros setores industriais: têxtil, processamento de café, extração de óleos vegetais e tratamento de águas residuárias (Jayani et al. 2005; Uenojo e Pastore, 2007). As pectinases podem ser obtidas por microrganismos, tanto em cultivo submerso como em estado

show abstract

Assessment of pectinase production by Aspergillus oryzae in growth-limiting liquid medium under limited and non-limited oxygen supply

Cited by 29 publications

References 27 publications

Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae

Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae

Enzyme-Assisted Extraction of Oil from Wet Microalgae Scenedesmus sp. G4

CARACTERIZAÇÃO DE EXTRATO PECTINOLÍTICO PRODUZIDO POR Aspergillus oryzae IPT-301

Contact Info

Product

Resources

About