Production and characterization of pectinase enzyme from Penicillium chrysogenum

Banu, A. Rasheedha; Devi, M. Kalpana; Gnanaprabhal, G. R.; Pradeep, B. V.; Palaniswamy, Muthusamy

doi:10.17485/ijst/2010/v3i4.10

Cited by 76 publications

(39 citation statements)

References 24 publications

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“…Pectinase from Aspergillus species have been reported to inactive due to denaturation at temperature above 50 °C (Galiotou-Panayotou et al 1997 ). However, the result obtained is in agreement with the pectinase enzyme produced by Penicillium chrysogenum , and a thermophilic fungus Aspergillus fumigatus which showed that the optimum pectinase activity at 50 °C (Banu et al 2010 ; Phutela et al 2005 ). Similarly pectinase enzyme from Aspergillus niger URM4645 is active at 50–80 °C and Thermomucorindicae_seudaticae N31 at 60 °C (Maciel et al 2011 ; Martin et al 2010 ).…”

Section: Discussionsupporting

confidence: 84%

“…The isolated pectinase activity was highly activated by Cd +2 (more than 50 %) followed by Mg +2 , Ba +2 and Fe +3 . Whereas, the pectinase activity from Penicillium chrysogenum was inhibited by 5 mM Mg +2 and Ba +2 ions (Banu et al 2010 ). This suggests that the requirement of metal ions for the pectinase activity vary depending upon their sources.…”

Section: Discussionmentioning

confidence: 99%

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Alkaline thermostable pectinase enzyme from Aspergillus niger strain MCAS2 isolated from Manaslu Conservation Area, Gorkha, Nepal

et al. 2015

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Pectinase enzymes are one of the commercially important enzymes having great potential in various industries especially in food industry. Pectinases accounts for 25 % of global food enzymes produced and their market is increasing day by day. Therefore, the exploration of microorganism with novel characteristics has always been the focus of the research. Microorganism dwelling in unique habitat may possess unique characteristics. As such, a pectinase producing fungus Aspergillus niger strain MCAS2 was isolated from soil of Manaslu Conservation Area (MCA), Gorkha, Nepal. The optimum production of pectinase enzyme was observed at 48 h of fermentation. The pectinase enzyme was partially purified by cold acetone treatment followed by Sephadex G-75 gel filtration chromatography. The partially purified enzyme exhibited maximum activity 60 U/mg which was almost 8.5-fold higher than the crude pectinase. The approximate molecular weight of the enzyme was found to be 66 kDa as observed from SDS-PAGE. The pectinase enzyme was active at broad range of temperature (30–70 °C) and pH (6.2–9.2). Optimum temperature and pH of the pectinase enzyme were 50 °C and 8.2 respectively. The enzyme was stable up to 70 °C and about 82 % of pectinase activity was still observed at 100 °C. The thermostable and alkaline nature of this pectinase can meet the demand of various industrial processes like paper and pulp industry, in textile industry, fruit juice industry, plant tissue maceration and wastewater treatment. In addition, the effect of different metal ions on pectinase activity was also studied.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Alkaline thermostable pectinase enzyme from Aspergillus niger strain MCAS2 isolated from Manaslu Conservation Area, Gorkha, Nepal

et al. 2015

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“…(35) labeled that finest temperature to pectinase manufacture from ( A. falvus ) was at ( 35°C). (36) empirical that pectinase manufacture from (P. chrysogenum )was progressive at ( 35°C).…”

Section: -6 Influence From Changed Temperature Going On Enzyme Actiomentioning

confidence: 99%

Investigation for Pectinase Pathogenicity & Activity of Mycological disease (Leaf Spot) in Solanum lycopersicum

Mezeal¹,

Hussin²

2019

التحديات الجيوفيزيائية والاجتماعية والانسانية والطبيعية في بيئة متغيرة

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Pathogenic ability of many fungal species qualified for nine of genera were recognized. (8) fungi were optimistic and positively talented to contaminate leaves of tomato seeming contamination indicators for the disease (leaf spot). Alternaria citri Alternaria alternata , Alternaria tenuissima , Botrytis cinerea , Botrytis squamosa were extremely infectious and formed this desease in most of infested leaves. Consequences protest this , in unhealthy plant life by Alternaria citri the chlorophyll was tremendously communicable presented maximum ominously condensed in (1.16-0.18) (mg/g fresh leaves) for chlorophyll(a, b) individually associated in (2-1.50) (mg/g fresh leaves) in controller plants. Alternaria alternate also march exciting condensed for chlorophyll (a, b) were (1. 89-0.98) (mg/g fresh leaves) correspondingly. (6) species were divided to capabilities to products pectinase by (cup-plate) technique. Totally mycological verified remained (pectinase) inventors then through adaptable shades. (3)species displayed in height pectinase inactivity include(Alternaria citri, Alternaria tenuissima and Alternaria alternaria) were(29, 26 and 23 mm) correspondingly, further species were create to be practical pectinase action include(Mycosphaerella tassiana, Botrytis squamosal , Botrytis cinerea). Pectinase formed by Alternaria citri increased by increasing of incubation

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“…Sisi aktif dari pektinase atau poligalakturonase yaitu residu asam amino aspartat dan histidin. Enzim pektinase dapat diisolasi dari Aspergillus niger, Bacillus coagulans, Bacillus firmus, Bacillus subtilis, Penicillium chrysogenum [2].…”

Section: Pendahuluanunclassified

Effect of Adding Ions - Metal Ions to Pectinase Activity Isolation from Bacillus Subtilis on Bleaching Paper

Putri

Roosdiana

Prasetyawan

et al. 2013

Nat-B

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Enzim pektinase digunakan sebagai biokatalis untuk merombak senyawa pektat atau pektin. Aktivitas pektinase di pengaruhi oleh ion-ion logam. Tujuan penelitian ini yaitu menentukan pengaruh penambahan ion-ion logam terhadap aktivitas pektinase dan menentukan jenis inhibisinya. Penentuan aktivitas enzim didasarkan pada pembentukan asam galakturonat, dianalisis secara spektrofotometri dengan pereaksi DNS. Pengaruh ion diuji dengan variasi konsentrasi ion logam Zn 2+ , Cu 2+ , Fe 3+ masingmasing 2-10 mM. Nilai Vm dan KM tanpa penambahan ion berturut-turut 161,29 µmol/mLmenit dan 0,55%(b/v). Sedangkan nilai Vmapp untuk penambahan ion Zn 2+ , Cu 2+ , Fe 3+ berturut-turut 147,06 µg.ml-1 , 156,25µg.ml-1 dan 153,85µg.ml-1. Nilai KMapp dari penambahan ion Zn 2+ , Cu 2+ , Fe 3+ yaitu 0,56%, 0,63%, dan 0,65%. Nilai KI berturut-turut untuk ion logam Zn 2+ , Cu 2+ dan Fe 3+ yaitu 333,33; 41,38; 32,97. Inhibisi untuk ketiga ion yaitu inhibisi non-kompetitif.

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Production and characterization of pectinase enzyme from Penicillium chrysogenum

Cited by 76 publications

References 24 publications

Alkaline thermostable pectinase enzyme from Aspergillus niger strain MCAS2 isolated from Manaslu Conservation Area, Gorkha, Nepal

Alkaline thermostable pectinase enzyme from Aspergillus niger strain MCAS2 isolated from Manaslu Conservation Area, Gorkha, Nepal

Investigation for Pectinase Pathogenicity & Activity of Mycological disease (Leaf Spot) in Solanum lycopersicum

Effect of Adding Ions - Metal Ions to Pectinase Activity Isolation from Bacillus Subtilis on Bleaching Paper

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