Production, Purification, and Characterization of Polygalacturonase from<i>Mucor circinelloides</i>ITCC 6025

Thakur, Abhishek; Pahwa, Roma; Singh, Smarika; Gupta, Reena

doi:10.4061/2010/170549

Cited by 55 publications

(43 citation statements)

References 36 publications

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“…Similar temperature optimum has been reported for PG from R. oryzae (Yadav et al 2012). Several fungal PGs exhibit temperature optima between 40 and 60°C (Devi and Rao 1996;Kaur et al 2004;Tari et al 2008;Thakur et al 2010). PG produced by few thermophilic fungal Fig.…”

Section: Effect Of Ph On the Activity And Stability Of Pgmentioning

confidence: 53%

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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Section: Effect Of Ph On the Activity And Stability Of Pgmentioning

confidence: 53%

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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“…The pH stability for 4 hours in the pH range 3.5-7.0 for PG produced by Mucor circunelloids ITCC 1065 has been reported (Thakur et al 2010). …”

Section: )mentioning

confidence: 99%

“…Several fungal PGs exhibit temperature optima between 40-60 • C (Devi et al 1996;Kaur et al 2004;Tari et al 2008;Thakur et al 2010). PG produced by a few thermophilic fungal strains, such as Thermoascus aurarifiacus, Aspergillus aculeatus and Fusarium oxysporum have temperature optima in the range 60-65…”

Section: )mentioning

confidence: 99%

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

et al. 2012

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An acidic polygalacturonase (PG) secreted by Rhizopus oryzae MTCC-1987 in submerged fermentation condition has been purified to electrophoretic homogeneity using ammonium sulphate fractionation and anion exchange chromatography on diethylaminoethyl cellulose. The purified enzyme gave a single protein band in sodium dodecyl sulphatepolyacrylamide gel electrophoresis analysis with a molecular mass corresponding to 75.5 kDa. The Km and kcat values of the PG were 2.7 mg/mL and 2.23 × 10 3 s −1 , respectively, using citrus polygalacturonic acid as the substrate. The optimum pH of the purified PG was 5.0 and it does not loose activity appreciably if left for 24 hours in the pH range from 5.0 to 12.0. The optimum temperature of purified enzyme was 50• C and the enzyme does not loose activity below 30• C if exposed for two hours. The purified enzyme showed complete inhibition with 1 mM Ag + , Hg 2+ and KMnO4, while it was stimulated to some extent by Co 2+ . The purified PG exhibited retting of Crotalaria juncea fibre in absence of ethylenediaminetetraacetic acid.

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“…Pectinase production used in industry has been reported from microorganisms including bacteria (Swain and Ray, 2010;Roosdiana et al, 2013), actinomycetes (Kuhad et al, 2004;Jacob and Prema, 2006), filamentous fungi in particular of the Aspergillus niger (Solis-Pereira et al, 1993), Penicillium pinophlilum (Ahmed and Mostafa, 2013), Penicillium viridicatum (Silva et al, 2002), Mucor circinelloides (Thakur et al, 2010) and some yeast (da Silva et al, 2005;Oliveira et al, 2006;Serrat et al, 2011;Taskin, 2013). Aspergillus niger is known worldwide for production of secondary metabolites and extracellular enzymes of commercial value, including industrial production of pectinases Yeasts have advantages compared to filamentous fungi with regard to the production of pectinases, because they are unicellular, the growth is relatively simple and the growth medium does not require an inducer.…”

Section: Introductionmentioning

confidence: 99%

Screening of Yeast Strains for Pectinolytic Activity: Effects of Different Carbon and Nitrogen Sources in Submerged Fermentations

Oskay¹,

Yalçın²

2015

OnLine Journal of Biological Sciences

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Twenty yeast strains were screened for pectinolytic activity, among the strains, only nine were positive for pectinase production. The best strain was Kluyveromyces marxianus NRRL-Y-1109 which gave high quantities of pectinase activity, by submerged fermentation. Different parameters such as incubation time, pH (3.5-7), temperature (20-45°C), nitrogen and carbon source, were optimized. The optimal incubation time, temperature and pH for pectinase production were found to be 48 h, 30°C and 6, respectively. Studies were conducted on the production of pectinase in submerged fermentation using agro-industrial residues such as wheat bran, grape waste, brewer's malt, beet molasses and corncob at a concentration of 1.5% (wt./vol.). Under optimized fermentation conditions, maximal enzyme were produced when citrus pectin (4.8 U/mL) was used as the carbon source, but high enzyme production was also obtained on wheat bran (2.2 U/mL) and grape waste (1.8 U/mL) in shaking conditions (120 rpm) for 48 h. Peptone and yeast extract used together as nitrogen source gave best enzyme production. The effects of temperature (30-70°C), pH (3.5-8) and salt concentration (1, 2, 5 and 10%) on the pectinase activity were determined. The optimum activity was obtained when temperature 45°C and pH at 5.5. The enzyme was stable at 45°C for more than 50 min, suggesting that it is relatively thermostable and being of interests for food processing.

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Production, Purification, and Characterization of Polygalacturonase fromMucor circinelloidesITCC 6025

Cited by 55 publications

References 36 publications

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

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

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

Screening of Yeast Strains for Pectinolytic Activity: Effects of Different Carbon and Nitrogen Sources in Submerged Fermentations

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