Variation of polygalacturonase and pectinesterase synthesis by aggregated mycelium of Aspergillus niger in dependence on the carbon source

Leuchtenberger, A.; Friese, E.; Ruttloff, H.

doi:10.1007/bf01031573

Cited by 13 publications

(5 citation statements)

References 3 publications

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“…Similar results were obtained of many authors who described the use on different inexpensive carbon sources for better production of pectinolytic enzymes (Aguilar and Huitron, 1986;Maldonado and Navarro, 1986;Hours et al, 1988;Larious et al, 1989;Leuchtenberger et al, 1989;Pericin et al, 1992;Shevchik et al, 1992;Hang and Woodams, 1994;Berovic and Ostroversnik, 1997;Alkorta et al, 1998;Zheng et al, 2000;Kaur and Satyanarayana, 2004;Joshi et al, 2006;Zhong-Tao et al, 2009;Tsereteli et al, 2009).…”

Section: Resultssupporting

confidence: 86%

“…Submerged fermentations generally produce smaller quantities of secretory enzymes and solid fermentations are not susceptible to automation. For the industrial production of pectinolytic enzymes it is important to improve the fermentation conditions, for better production of extracellular enzymes on inexpensive carbon sources such as apple pomace, citric peels, pectin or other agricultural wastes which contain appreciable quantities of pectin (Alkorta et al, 1998;Maldonado and Navarro, 1986;Leuchtenberger et al, 1989;Aguilar and Huitron, 1986;Larious et al, 1989;Akinyele et al, 2010). The most authors describe the use of an optimized medium composition to increase the enzyme content (Pericin et al, 1992;Berovic and Ostroversnik, 1997;Shevchik et al, 1992;Tsereteli et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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The effects of different carbon sources on biosynthesis of pectinolytic enzymes by Aspergillus niger

Mojsov¹

2010

ATI

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The aim of this work was to investigate the effects of different carbon sources on the nourishing base on the production of pectinolytic enzymes by Aspergillus niger with the aim of optimizing the medium for maximal enzyme production.Growth and enzymes production by Aspergillus niger were evaluated on glucose, fructose, galactose, xylose, lactose, apple pectin and the dry apple pulp. Results of different carbon sources on base showed maximal endo-pectinolytic activity, endo-PG

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Section: Resultssupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

The effects of different carbon sources on biosynthesis of pectinolytic enzymes by Aspergillus niger

Mojsov¹

2010

ATI

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“…Submerged fermentation generally produces smaller quantities of secretory enzymes and solid fermentations is not susceptible to automation. For the industrial production of pectinolytic enzymes it is important to improve fermentation conditions, for better production of extracellular enzymes in liquid culture on inexpensive carbon sources such as apple pomace, citric peels, pectin or other agricultural wastes (Leuchtenberger et al, 1989;Aguilar and Huitron, 1986;Larios et al, 1989). The most authors describe the use of an optimized medium composition to increase the enzyme content (Pericin et al, 1992;Acuna-Arguelles et al, 1995;Berovic and Ostroversnik, 1997).…”

Section: Introductionmentioning

confidence: 99%

Experimental investigations of submerged fermentation and synthesis of pectinolytic enzymes by Aspergillus Niger : Effect of inoculum size and age of spores

Mojsov

2010

ATI

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The paper investigates effects of the different concentration of inoculums and age of spores in the synthesis of pectinolytic enzymes with the aim of their optimizing for maximal enzyme production and growth of the microorganism. The microorganism used in this work was the fungus Aspergillus niger MK-15, which was isolated from soil as a highly active producer of pectinolytic enzymes. The results showed that the concentration of the inoculum and age of spores have a pronounced effect on the pectinolytic activity and dry weight. Obrained results sugest that for submerged fermentation and synthesis of pectinolytic enzymes by Aspergillus niger MK-15, the optimal inoculum concentration is 3% or 6x106 spores and optimal age of spores is 3 days old.

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“…Pectin-degrading enzymes are produced by many plant-associated micro-organisms and several saprophytes. Pectic enzymes have been reported from many molds such as species of Aspergillus [2], Cladosporium [3], Fusarium [4,5], Geotrichum [6], Penicillium [7] and Sclerotina [8]. Pectic polymers, consisting predominantly of 1,4-linked -galacturonic acid and methoxylated derivatives, are major constituents of the middle lamellae and primary cell walls of higher plants [9].…”

Section: Introductionmentioning

confidence: 99%

Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae

Rao

Kembhavi

Pant

1996

Biochemical Journal

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An extracellular pectate lyase from Fusarium moniliformae was purified to homogeneity by affinity chromatography followed by gel filtration, with a yield of 76.5%. Laser desorption MS of the enzyme gave a molecular mass of 12,133.5 +/- 2.5 Da. The pectate lyase was a glycoprotein with a 5% carbohydrate content and had a pl value of 9.1. Atomic-emission spectrometry showed that Ca2+ was a part of the holoenzyme held by carboxy groups of the protein. These results support the hypothesis of a putative Ca2+ site suggested by Yodder, Keen and Jurnak [(1993) Science 260, 1503-1507] in the crystal structure of pectate lyase C of Erwinia chrysanthemi. Loss of Ca2+ was observed by treatment with EGTA or carboxy-modifying Woodward's reagent K, with subsequent loss of enzyme activity. Tryptophan fluorescence quenching showed that Ca2+ does not affect binding of substrate to enzyme. Chemical-modification and substrate-protection studies showed the presence of lysine and tryptophan at or near the active site of the pectate lyase. Chemically modified enzyme showed no major structural changes as determined by CD. Amino acid analyses of native, trinitrobenzenesulphonate (TBNS)-treated and substrate-protected TNBS-treated enzyme showed that a single essential residue of lysine is present at or near the active-site. Substrate-affinity studies showed that tryptophan could be essential for substrate binding, whereas lysine could be involved in the catalysis. Fluorescence quenching further confirmed the involvement of tryptophan in substrate binding. The reaction mechanism involving beta-elimination by this enzyme is discussed.

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Variation of polygalacturonase and pectinesterase synthesis by aggregated mycelium of Aspergillus niger in dependence on the carbon source

Cited by 13 publications

References 3 publications

The effects of different carbon sources on biosynthesis of pectinolytic enzymes by Aspergillus niger

The effects of different carbon sources on biosynthesis of pectinolytic enzymes by Aspergillus niger

Experimental investigations of submerged fermentation and synthesis of pectinolytic enzymes by Aspergillus Niger : Effect of inoculum size and age of spores

Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular-mass pectate lyase from Fusarium moniliformae

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