Kinetic properties and thermal behaviour of polygalacturonase used in fruit juice clarification

Ortega, Natividad; Diego, S. de; Pérez-Mateos, M.; Busto, María D.

doi:10.1016/j.foodchem.2004.01.035

Cited by 116 publications

(87 citation statements)

References 32 publications

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“…This value is in the range of the values (40-70 kcal mol −1 ) estimated for many microbial enzymes [16]. The inactivation energy estimated for this enzyme was 1.96, 1.71 and 1.77 times higher than the commercial exo-polygalacturonases like Rapidase C80, Pectinase CCM and Pectinex 3XL, respectively, compared to a study conducted by Ortega et al [27]. These close approximations with the current commercial enzymes indicated that the purified enzyme could be a good candidate for various industrial applications.…”

Section: Kinetics Of Thermal Inactivation and Estimation Of The Inactsupporting

confidence: 46%

“…of an exo-polygalacturonase from A. niger as 60 • C, similarly, maximum activity for commercial enzyme, Rapidase C80 was determined at 55 • C [27]. Furthermore, the partially purified polygalacturonase from Sporotrichum thermophile Apinis was optimally active at 55 • C as well [3,4].…”

Section: Effect Of Temperature On Exo-polygalacturonase Activity and mentioning

confidence: 71%

“…This indicates that the current exopolygalacturonase has a higher affinity for PGA compared to the other two. Similarly, the current exo-polygalacturonase had 1.38, 1.47 and 1.65 times more affinity towards PGA substrate than the commercial enzymes Rapidase C80, Pectinase CCM and Pectinex, respectively jugged from the K m values [27]. V m which is an indication of the catalytic activity of an enzyme is usually desired to be as high as possible, therefore the cur- rent value obtained in this study was very comparable to many studies in the literature [27,30].…”

Section: Calculation Of Kinetic Constantsmentioning

confidence: 78%

“…In order to increase productivity and reduce microbial contaminations, industrial processes may require reactions carried out at high temperatures. That is why thermostable enzymes have been the target of many studies involving the elucidation of thermal inactivation mechanism and development of strategies for stability enhancement [27]. Therefore, the current exo-polygalacturonase in this study will exhibit a new example for thermostable enzymes obtained from a new source (A. sojae) with unique properties.…”

Section: Effect Of Temperature On Exo-polygalacturonase Activity and mentioning

confidence: 99%

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Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Dogan¹,

Tarı²

2008

Biochemical Engineering Journal

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Exo-polygalacturonase enzyme produced by Aspergillus sojae ATCC 20235 was purified using three-phase partitioning (TPP), an emerging bio-separation technique where a single step as compared to the classical multi-step purification was used. Using this technique, crude enzyme solution (pH 6.6) saturated to 30% (w/v) with ammonium sulphate and with a crude extract to tert-butanol ratio of 1:1 (v/v) at 25• C resulted in 25.5% recovery of exo-polygalacturonase with a 6.7-fold purification. The purified enzyme was characterized with respect to its activity and stability at various pH and temperature ranges. Optimum pH and temperature for maximum activity were determined as pH 4 and 55• C. The enzyme was stable at both acidic and alkaline pH for 2 h at 30• C. The thermal stability study showed that the purified enzyme had an inactivation energy of 68.41 kcal/mol and a half-life (t 1/2 ) value of 3.6 h at 75• C presenting a large thermal stability. The kinetic constants K m and V max using polygalacturonic acid as substrate were 0.75 g l −1 and 1.14 mol min −1 , respectively. SDS-PAGE profiling revealed that the purified exopolygalacturonase had two bands with the molecular weights of 36 and 53 kDa. The enzyme was completely inhibited in the presence of Mn 2+ and SDS and induced significantly by EDTA, glycerol and ␤-mercaptoethanol.

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Section: Kinetics Of Thermal Inactivation and Estimation Of The Inactsupporting

confidence: 46%

Section: Effect Of Temperature On Exo-polygalacturonase Activity and mentioning

confidence: 71%

Section: Calculation Of Kinetic Constantsmentioning

confidence: 78%

Section: Effect Of Temperature On Exo-polygalacturonase Activity and mentioning

confidence: 99%

See 2 more Smart Citations

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Dogan¹,

Tarı²

2008

Biochemical Engineering Journal

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“…Altos valores de entalpia também são característicos da reação de desnaturação proteica. Valores de ∆S* próximos de zero, demonstram que a desnaturação térmica não necessariamente implica em variações na estrutura terciária da enzima 10 .…”

Section: Bbr -Biochemistry and Biotechnology Reports -Issn 2316-5200 unclassified

Propriedades Termodinâmicas da Enzima Beta-Galactosidase Imobilizada em Eupergit® C

Braga¹,

Silveira²,

Kalil³

2013

BBR - Biochem. Biotechnol.

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INTRODUÇÃOA β-galactosidase é uma enzima hidrolítica com capacidade de transferase para grupos galactosil, atuando no resíduo terminal β-galactopiranosil da lactose para formar seus monossacarídeos glicose e galactose. É utilizada na indústria farmacêutica e alimentícia principalmente na elaboração de produtos destinados a pessoas com intolerância à lactose 1 . A lactose é um dissacarídeo que tem como características principais, baixa solubilidade em água e baixo poder adoçante. A cristalização deste açúcar em produtos lácteos, como leite condensado, e a restrição ao consumo de tais alimentos por pessoas intolerantes a este carboidrato, devido a baixos níveis de β-galactosidase intestinal, podem ser evitadas através do processo de hidrólise enzimático 1 . Dentre as fontes de β-galactosidase destacam-se aquelas obtidas por micro-organismos, principalmente a partir de leveduras do gênero Kluyveromyces, que são considerados seguros, podendo ser utilizados na área de alimentos 2,3 . A imobilização de β-galactosidase é uma ferramenta muito poderosa para melhorar quase todas as suas propriedades, incluindo estabilidade, atividade, seletividade, especificidade e redução de inibição 4 . Nesse contexto, o objetivo desse trabalho foi determinar algumas propriedades enzimáticas da enzima β-galactosidase parcialmente purificada e imobilizada, utilizando Eupergit ® C como suporte. MATERIAL E MÉTODOS Produção, Extração e Purificação da enzima β-galactosidase

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Fungal biomolecules for the food industry

Nguyen

Bujna

Styevkó

et al. 2015

Fungal Biomolecules

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Kinetic properties and thermal behaviour of polygalacturonase used in fruit juice clarification

Cited by 116 publications

References 32 publications

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Propriedades Termodinâmicas da Enzima Beta-Galactosidase Imobilizada em Eupergit® C

Fungal biomolecules for the food industry

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