Two thermophilic fungal pectinases from Neosartorya fischeri P1: Gene cloning, expression, and biochemical characterization

Li, Ke; Meng, Kun; Pan, Xin; Ma, Rui; Yang, Peilong; Huang, Huoqing; Yao, Bin; Su, Xiaoyun

doi:10.1016/j.molcatb.2015.05.005

Cited by 16 publications

(12 citation statements)

References 46 publications

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“…This result confirmed that the enzyme is an endo-polygalacturonase. Similar results were reported earlier by Li et al [22] and Doostdar et al [38]. …”

Section: Product Identificationsupporting

confidence: 93%

Purification and Characterization of Polygalacturonase Produced by Aspergillus niger AN07 in Solid State Fermentation

Patidar¹,

Nighojkar²,

Nighojkar³

et al. 2017

Can J Biotech

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“…This result confirmed that the enzyme is an endo-polygalacturonase. Similar results were reported earlier by Li et al [22] and Doostdar et al [38]. …”

Section: Product Identificationsupporting

confidence: 93%

Purification and Characterization of Polygalacturonase Produced by Aspergillus niger AN07 in Solid State Fermentation

Patidar¹,

Nighojkar²,

Nighojkar³

et al. 2017

Can J Biotech

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“…Di-nitro salicylic acid (DNS) method is commonly used for determination of polygalacturonase activity. It is used to determine the amount of reducing sugars (galacturonic acid) released from the polygalacturonic acid substrate (Miller 1959;Li et al 2015). In this method, after incubation, DNS solution is added in the reaction mixture to stop the reaction and tubes are kept in boiling water for 15 min (Jayani et al 2005).…”

Section: Di-nitro Salicylic Acid Methods (Miller's Method)mentioning

confidence: 99%

“…Enzyme activity can be calculated using following formula (Li et al 2015) where "v" is the enzyme volume used in the assay, "194.1" is the molecular weight of galacturonic acid, and t is the reaction time in min.…”

Section: Di-nitro Salicylic Acid Methods (Miller's Method)mentioning

confidence: 99%

Pectinolytic enzymes-solid state fermentation, assay methods and applications in fruit juice industries: a review

Patidar

Nighojkar²,

Kumar

et al. 2018

3 Biotech

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A plethora of solid substrates, cultivation conditions and enzyme assay methods have been used for efficient production and estimation of polygalacturonase and pectin methylesterase enzymes. Recent developments in industrial biotechnology offer several opportunities for the utilization of low cost agro-industrial waste in Solid State Fermentation (SSF) for the pectinolytic enzyme production using fungi. Fruit waste mainly citrus fruit waste alone and along with other agro-industrial waste has been explored in SSF for enzyme production. Agro-industrial waste, due to the economic advantage of low procuring cost has been employed in SSF bioreactors for pectinolytic enzyme production. Acidic pectinases produced by fungi are utilized especially in food industries for clarification of fruit juices. This review focuses on the recent developments in SSF processes utilizing agro-industrial residues for polygalacturonase and pectin methylesterase production, their various assay methods and applications in fruit juice industries.

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“…Therefore, Pel4J4 is a promising application prospect in ramie bio-degumming. 26 The effects of 1 mmol/L metal ions on the enzyme activity are shown in Table 4. The enzyme activity was promoted by Zn 2+ , Fe 3+ , Ca 2+ , and NH þ 4 but significantly inhibited by Cu 2+ and Pb 2+ , while Ni 2+ , Mn 2+ , and K + had no significant effects on the enzyme activity.…”

Section: Enzyme Properties Of Pel4j4mentioning

confidence: 99%

An alkaline pectate lyase D from Dickeya dadantii DCE-01: clone, expression, characterization, and potential application in ramie bio-degumming

Cheng

Duan

Zheng

et al. 2018

Textile Research Journal

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Pectinase plays a crucial role in ramie bio-degumming. A pectate lyase gene ( pel4J4) from the high-efficiency degumming bacteria Dickeya dadantii DCE-01 of bast fibers was cloned and connected to pET28a, and then the recombinant plasmid was successfully transformed into Escherichia coli BL21(DE3). The pectate lyase (Pel4J4) induced was purified by ultrafiltration and Sephadex G-100 gel chromatography. The enzymatic properties of Pel4J4 were studied in detail. pel4J4 (GenBank accession number: KC900167) had a sequence length of 1179 bp, encoding 392 amino acids. The extracellular pectate lyase activity of pET28a- pel-BL was up to 204.4 IU/mL. The optimal temperature and pH of the purified Pel4J4 were 55℃ and 8.5, respectively. The stable temperature and pH of Pel4J4 activity were 45℃ and 8.5–10.0, respectively. The catalytic activity is Ca2+ dependent and promoted by 1 mmol/L Zn2+, Fe3+, Ca2+, and NH4+, but seriously inhibited by Cu2+ and Pb2+. The optimal substrate is citrus pectin with more than 85% esterification. The heat-resistant alkaline Pel4J4 could strongly degrade natural ramie pectin, indicating a promising application prospect in ramie bio-degumming.

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Two thermophilic fungal pectinases from Neosartorya fischeri P1: Gene cloning, expression, and biochemical characterization

Cited by 16 publications

References 46 publications

Purification and Characterization of Polygalacturonase Produced by Aspergillus niger AN07 in Solid State Fermentation

Purification and Characterization of Polygalacturonase Produced by Aspergillus niger AN07 in Solid State Fermentation

Pectinolytic enzymes-solid state fermentation, assay methods and applications in fruit juice industries: a review

An alkaline pectate lyase D from Dickeya dadantii DCE-01: clone, expression, characterization, and potential application in ramie bio-degumming

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