Enzymes with new biochemical properties in the pectinolytic complex produced by Aspergillus niger MIUG 16

Dinu, Diana; Nechifor, Marina Tamara; Stoian, Gheorghe; Costache, Marieta; Dinischiotu, Anca

doi:10.1016/j.jbiotec.2007.06.005

Cited by 62 publications

(44 citation statements)

References 39 publications

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“…For the Panzym Clears commercial pectinase sample at constant temperature 45 °C, it was also observed that the maximum PME activity was at pH 4.0. These data is in agreement with those reported by Duvetter et al (2005), Dinu et al (2007) for commercial pectinase samples obtained from Aspergillus aculeatus and niger. Figure 3 shows the temperature influence on the PME activity of Pectinex 100 L Plus keeping the pH constant at 4.0.…”

Section: Pme Activity Through Naoh Volume Variationsupporting

confidence: 93%

Determination of pectin methylesterase activity in commercial pectinases and study of the inactivation kinetics through two potentiometric procedures

Gonzalez¹,

Rosso²

2011

Ciênc. Tecnol. Aliment.

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Section: Pme Activity Through Naoh Volume Variationsupporting

confidence: 93%

Determination of pectin methylesterase activity in commercial pectinases and study of the inactivation kinetics through two potentiometric procedures

Gonzalez¹,

Rosso²

2011

Ciênc. Tecnol. Aliment.

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“…Submerged fermentation (SmF) and solid state fermentation (SSF) have been successfully used in pectinase production by fungi [18,[70][71][72] and by bacteria [16,33,34,36,73].…”

Section: Microbial Pectinasesmentioning

confidence: 99%

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

Pedrolli¹,

Monteiro²,

Gomes³

et al. 2009

TOBIOTJ

274

123

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Pectinases are a big group of enzymes that break down pectic polysaccharides of plant tissues into simpler molecules like galacturonic acids. It has long been used to increase yields and clarity of fruit juices. Since pectic substances are a very complex macromolecule group, various pectinolytic enzymes are required to degrade it completely. These enzymes present differences in their cleavage mode and specificity being basically classified into two main groups that act on pectin "smooth" regions or on pectin "hairy" regions. Pectinases are one of the most widely distributed enzymes in bacteria, fungi and plants. This review describes the pectinolytic enzymes and their substrates, the microbial pectinase production and characterization, and the industrial application of these enzymes.

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“…In general, both submerged state fermentation (SmF) and solid-state fermentation (SSF) have been successfully used in pectinases production from different microbial strains (Castilho et al 2000;Silva et al 2002;Pedrolli and Carmona 2009;Dinu et al 2007). The solid-state fermentation is preferred over submerged fermentation based on the fact that it uses various agro-industrial by-products such as soy, pulps of apple, sugar beet and coffee, peels of lemon, oranges and tomato, pomace of apple and citrus fruits, sugarcane bagasse, wheat bran, etc., making the entire process cost effective (Castilho et al 2000;Yadav and Shastri 2007;Lara-Marquez et al 2011;Yadav et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Production, purification and biochemical characterization of an exo-polygalacturonase from Aspergillus niger MTCC 478 suitable for clarification of orange juice

Anand

Yadav

2017

3 Biotech

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Polygalacturonases (PG) represent an important member of pectinases group of enzymes with immense industrial applications. A fungal strain Aspergillus niger MTCC478 was used for the production of polygalacturonase both under submerged and solid-state fermentation condition. Further its production was optimized under solid-state fermentation condition with media comprising of wheat bran and tea extract. Purification of an exo-PG was achieved by acetone precipitation (60-90%) and CMcellulose column chromatography revealing 15.28-fold purification with a specific activity of 33.47 U/mg protein and 1.2% yield. A relative molecular mass of purified PG was approximately 124.0 kDa. The pH and temperature optimum was found to be 4 and 50°C, respectively. The k cat and K m value for degradation of PGA by the purified enzyme was found to be 194 s -1 and 2.3 mg/mL, respectively. Cu 2? was found to enhance the PG activity while Ag ? completely inhibited the enzyme activity. The application of the purified PG in orange juice clarification was elucidated.

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Enzymes with new biochemical properties in the pectinolytic complex produced by Aspergillus niger MIUG 16

Cited by 62 publications

References 39 publications

Determination of pectin methylesterase activity in commercial pectinases and study of the inactivation kinetics through two potentiometric procedures

Determination of pectin methylesterase activity in commercial pectinases and study of the inactivation kinetics through two potentiometric procedures

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

Production, purification and biochemical characterization of an exo-polygalacturonase from Aspergillus niger MTCC 478 suitable for clarification of orange juice

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