Isolation and characterization of extracellular pectin lyase from Penicillium canescens

Синицына, О. А.; Федорова, Э. А.; Семенова, М. В.; Gusakov, Alexander V.; Соколова, Л. М.; Bubnova, T. M.; Окунев, О. Н.; Чулкин, А. М.; Вавилова, Е. А.; Vinetsky, Yu. P.; Sinitsyn, A. P.

doi:10.1134/s0006297907050148

Cited by 32 publications

(17 citation statements)

References 19 publications

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“…The obtained results on the study of stability of PEL A and PG at 20, 50, and 85°C (Table 4) coincided with the literature data [16][17][18][19][20]. CBH and EG from P. verrucu losum were more stable at 50 and 60°C as compared to PEL A and PG.…”

Section: Resultssupporting

confidence: 87%

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Developing the producers of cellulolytic and pectinolytic enzymes based on the fungus Penicillium verruculosum

Bushina

Рубцова

Рожкова

et al. 2015

Appl Biochem Microbiol

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Based on the fungus Penicillium verruculosum, we created strains with a complex of extracellular enzymes that contains both cellulolytic enzymes of the fungus and heterologous pectin lyase A from P. cane scens and endo 1,4 α polygalacturonase from Aspergillus niger. The endopolygalacturonase and pectin lyase activities of enzyme preparations obtained from culture media of the producer strains reached 46-53 U/mg of protein and 1.3-2.3 U/mg of protein, respectively. The optimum of temperature and pH for recombinant pectin lyase and endopolygalacturonase corresponded to those described in the literature for these enzymes. The content of heterologous endopolygalacturonase and pectin lyase in the studied enzyme preparations was 4-5% and 23% of the total protein content, respectively. The yield of reducing sugars upon the hydrolysis of sugar beet and apple processing wastes with the most efficient preparation was 41 and 71 g/L, respectively, which corresponded to a polysaccharide conversion of 49% and 65%. Glucose was the main product of the hydrolysis of sugar beet and apple processing wastes.

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Section: Resultssupporting

confidence: 87%

“…It should be noted that PEL A and PG at 40°C turned out to be more stable in the obtained EPs than the enzymes described in the literature [16][17][18][19][20]. The obtained results on the study of stability of PEL A and PG at 20, 50, and 85°C (Table 4) coincided with the literature data [16][17][18][19][20].…”

Section: Resultssupporting

confidence: 85%

Developing the producers of cellulolytic and pectinolytic enzymes based on the fungus Penicillium verruculosum

Bushina

Рубцова

Рожкова

et al. 2015

Appl Biochem Microbiol

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“…PLs do not have an absolute requirement of Ca 2+ but they are stimulated by this and other cations [6]. Up until now, all described pectin lyases are endo-PLs (EC 4.2.2.10) [28]. Van Alebeek and coworkers [29] conducted a detailed study of the action mode of pectin lyase A from Aspergillus niger which produces mono-, di-, tri-and tetragalacturonates, besides unsaturated di-, tri-and tetragalacturonates from methyloligogalacturonates.…”

Section: Pectin Lyases (Pl)mentioning

confidence: 99%

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

Pedrolli¹,

Monteiro²,

Gomes³

et al. 2009

TOBIOTJ

287

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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“…2166.1 (ABN+PEL+PG series) was significantly shorter. It is known that native ABN from A. niger exhibits maximum activity at 51°C and remains stable at a pH of 4.6 and 50°C for at least 2 h, but it loses activity at a pH of 5.5-6.5 [18,19]. Hence, recombinant ABN displayed properties similar to the native enzyme of A. niger.…”

Section: Resultsmentioning

confidence: 99%

Novel enzyme preparations with high pectinase and hemicellulase activity based on Penicillium canescens strains

Рубцова

Bushina

Рожкова

et al. 2015

Appl Biochem Microbiol

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Recombinant strains of Penicillium canescens producing homologous pectin lyase A and heterol ogous endo 1,5 α arabinase A and endo 1,4-α polygalacturonase, as well as enzymes of the host strain (α L arabinofuranosidases, xylanases, and others), were obtained by genetic engineering. The enzyme prep arations (EPs) obtained from the cultural medium of recombinant P. canescens strains efficiently hydrolyzed raw plant material with a high content of pectin compounds. It was shown that the yield of reducing sugars and arabinose increased 16 and 22% in comparison with the control EP based on the host strain when one of the obtained EPs was used for beet pulp hydrolysis. It was established that the most active EP consisted of pec tin lyase (10%), endo 1,5 arabinase (26%),α L arabinofuranosidase and arabinoxylan arabinofuranohy drolase (12%), and xylanase (10%). The activities of pectin lyase, polygalacturonase, and arabinase of the EP in reactions with various substrates were determined. The specificity, pH and T optima, and thermal stability of the homogenous recombinant endo 1,5 α arabinase were investigated. The kinetic parameters (K m , k cat ) of the linear arabinan hydrolysis were determined.

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Isolation and characterization of extracellular pectin lyase from Penicillium canescens

Cited by 32 publications

References 19 publications

Developing the producers of cellulolytic and pectinolytic enzymes based on the fungus Penicillium verruculosum

Developing the producers of cellulolytic and pectinolytic enzymes based on the fungus Penicillium verruculosum

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

Novel enzyme preparations with high pectinase and hemicellulase activity based on Penicillium canescens strains

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