Formation and release of pectin lyase during growth of Penicillium paxilli

Szajer, I.; Czajer, Cz.

doi:10.1007/bf01026679

Cited by 8 publications

(7 citation statements)

References 6 publications

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“…The temperature effect on P. italicum PNL activity consisted of an increase up to 50°C. This value is higher than those reported for filtrates of A. niger (34), Aureobasidium pullulans (16), B. cinerea (24), and P. paxilli (30,31), in which the maximum PNL activity is obtained at temperatures ranging from 35 to 40°C. PNL from P. italicum is more thermostable than other PNLs described for Penicillium culture filtrates (21,28,30,31), Aspergillus sojae (14), and C. lindemuthianum (33), in which thermoinactivation is observed in the range of 30 to 45°C.…”

Section: Discussioncontrasting

confidence: 68%

“…The effect of pH on the stability of PNL from P. italicum culture filtrates shows that this enzyme is more stable at high pH values. These results show a wider range of stability than that reported for P. paxilli (30,31), in which PNL is only stable in the pH range of 4.0 to 6.0. The stability shown by the P. italicum PNL activity after several months of storage at 4°C or freezing at -20°C is also remarkable.…”

Section: Discussioncontrasting

confidence: 44%

“…As previously reported (1), P. italicum grown in submerged culture produces an extracellular PNL, the production of which is induced at low pHs by the presence of highly esterified pectins. This PNL release is a common feature in filamentous fungi (23), although in Penicillium paxilli this activity has been found not only in the medium but also associated with the mycelium (31). Besides PNL, polygalacturonase is present in P. italicum culture filtrates, but PL and pectinesterase activities were not detected.…”

Section: Discussionmentioning

confidence: 89%

“…Several studies dealing with production and characterization of PNL have been done with Penicillium spp. over the last twenty years (6,7,21,28,30,31). Nevertheless, there is still a lack of information about PNL properties and possible applications of Penicillium culture filtrates.…”

mentioning

confidence: 99%

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Pectin Lyase Activity in a Penicillium italicum Strain

Alaña

Alkorta

Dominguez

et al. 1990

Appl Environ Microbiol

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An extracellular pectin lyase (PNL) [poly-(methoxygalacturonide)lyase; EC 4.2.2.10] produced by Penicillium italicum CECT 2294 grown on a surface bran (natural medium) or in a submerged (synthetic medium) culture was investigated. Both culture filtrates showed macerating activity at low pH on cucumber, potato, and orange tissues. The physicochemical properties of the enzyme obtained from both culture methods were identical, as well as its catalytic properties, which were assayed by different methods. The molecular mass of the PNL obtained by gel filtration chromatography was 22 kDa; the isoelectric point was 8.6, as determined by chromatofocusing; and the enzyme was able to catalyze the eliminative cleavage of pectins with low (37%) and high (from 54 to 82%) degrees of esterification. The PNL produced in liquid medium showed a K,m for pectin (degree of esterification, 70%) of 3.2 mg/ml, and the optimum pH was 6.0 to 7.0. This enzyme was stable at 50°C and at pH 8.0. The ability of this PNL to macerate plant tissues in acidic environmental conditions, its stability at low pH and temperatures up to 50°C (thus preventing mesophilic microbial growth), and the absence of pectinesterase make this preparation useful for the food industry.

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Section: Discussioncontrasting

confidence: 68%

Section: Discussioncontrasting

confidence: 44%

Section: Discussionmentioning

confidence: 89%

mentioning

confidence: 99%

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Pectin Lyase Activity in a Penicillium italicum Strain

Alaña

Alkorta

Dominguez

et al. 1990

Appl Environ Microbiol

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“…A number of evidences indicate a role of ambient pH in the regulation of production of pectinolytic enzymes in fungi such as Penicillium paxilli (Szajer and Czajer, 1985), P. itallicum (Alaña et al, 1989), the avocadopathogen C. gloeosporioides (Drori et al, 2003;KramerHaimovich et al, 2006;Yakoby et al, 2000), Trametes trogii (Levin and Forchiassin, 1998) and Aspergillus oryzae (Fontana and Silveira, 2012). In the latter, alkalinization during fruit infection is necessary for the conversion of the biotrophic stage into the necrotrophic stage (Kramer-Haimovich et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of an endo--1,4-xylanase gene from Colletotrichum lindemuthianum and phylogenetic analysis of similar genes from phytopathogenic fungus

Conejo-Saucedo¹,

Cano-Camacho²,

LÃ3pez-Romero³

et al. 2016

Afr. J. Microbiol. Res.

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Colletotrichum lindemuthianum is the etiological agent of anthracnose, one of the main diseases of bean (Phaseolus vulgaris). In this study, the complete cDNAs of two endo-β-1,4-xylanase genes (xyl1) from non-pathogenic (0) and pathogenic (1472) races of C. lindemuthianum were isolated and characterized. To get an insight into the role of endo-β-1,4-xylanases in their different lifestyles, xyl1 gene expression and enzyme activity in mycelia of both races grown in the presence of xylan or P. vulgaris cell walls were investigated. The xyl1 sequence analysis and Clustal alignment revealed the characteristic elements of genes coding for endo-β-1,4-xylanases of the GH11 family. The growth of the two races with glucose as the sole carbon source showed both basal transcription levels of xyl1 and endoxylanase activity. When glucose was substituted with xylan or plant cell walls, xyl1 transcription, and enzyme activity significantly increased in race 1472 as compared to race 0. The pathogenic race degraded xylan faster and grew better than the non-pathogenic counterpart. Seemingly, the regulation of xylanolytic gene expression, enzyme production and the nature of the assimilatory carbon substrates processed by these organisms play a determinant role in their lifestyle. Phylogenetic analyses of XYL1 and endo-β-1,4-xylanases from other fungi revealed a diversification process and separation of proteins from the same fungal species into different lineages.

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Production of ?-glycosidases (linamarase and amygdalase) and pectolytic enzymes by Penicillium spp.

Brimer¹,

Cicalini²,

Federici³

et al. 1994

World Journal of Microbiology & Biotechnology

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Fifty-eight strains, representing 31 species of Penicillium, were screened for extracellular β-glycosidase (amygdalase/linamarase) and pectolytic (polygalacturonase, pectin lyase) enzymes. One strain each of P. turbatum, P. piceum and P. paxilli showed very high β-glycosidase activity and slightly lower activities were found in P. crustosum, P. expansum, P. oxalicum and P. aurantiogriseum. Generally, maximum β-glycosidase activity showed reached during the stationary phase of growth. The seven species with highest β-glycosidase activity showed different patterns of pectolytic activities, indicating that different species or combinations of species could be selected for different potential applications.

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Formation and release of pectin lyase during growth of Penicillium paxilli

Cited by 8 publications

References 6 publications

Pectin Lyase Activity in a Penicillium italicum Strain

Pectin Lyase Activity in a Penicillium italicum Strain

Cloning and characterization of an endo--1,4-xylanase gene from Colletotrichum lindemuthianum and phylogenetic analysis of similar genes from phytopathogenic fungus

Production of ?-glycosidases (linamarase and amygdalase) and pectolytic enzymes by Penicillium spp.

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