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2015 | 18 | 4 |
Tytuł artykułu

Moulds lytic enzymes in the production of Yarrowia high-protein feed additives

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Wydawca
-
Rocznik
Tom
18
Numer
4
Opis fizyczny
http://www.ejpau.media.pl/volume18/issue4/art-04.html
Twórcy
autor
  • Department of Biotechnology and Food Microbiology, Wroclaw University of Environmental and Life Sciences, Chelmonskiego 37/41, 51-630 Wroclaw, Poland
  • Department of Biotechnology and Food Microbiology, Wroclaw University of Environmental and Life Sciences, Chelmon,skiego 37/41, 51-630 Wroclaw, Poland
  • Department of Biotechnology and Food Microbiology, Wroclaw University of Environmental and Life Sciences, Chelmonskiego 37/41, 51-630 Wroclaw, Poland
autor
  • Department of Biotechnology and Food Microbiology, Wroclaw University of Environmental and Life Sciences, Chelmonskiego 37/41, 51-630 Wrocław, Poland
autor
  • Department of Biotechnology and Food Microbiology, Wroclaw University of Environmental and Life Sciences, Chelmonskiego 37/41, 51-630 Wroclaw, Poland
Bibliografia
  • Bradford M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
  • El-Katatny M.H., Somitsch W., Robra K.H., El-Katatny M.S., Gübitz G.M., 2000. Production of chitinase and β-1,3-glucanase by Trichoderma harzianum for control of the phytopathogenic fungus Sclerotium rolfsii. Food Technology and Biotechnology, 38, 173–180.
  • El-Katatny M.H., Gudelj M., Robra K.H., Elnaghy M.A., Gübitz G.M., 2001. Characterization of a chitinase and an endo-β-1,3-glucanase from Trichoderma harzianum Rifai T24 involved in control of the phytopathogen Sclerotium rolfsii. Applied Microbiology and Biotechnology, 56, 137–143.
  • Fontaine T., Simenel C., Dubreucq G., Adam O., Delepierre M., Lemoine J., Vorgias C.E, Diaquin M., Latge J.P., 2000. Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall. Journal of Biological Chemistry, 275, 27594–27607.
  • Hanson L.E., Howell C.R., 2004. Elicitors of plant defense responses from biocontrol strains of Trichoderma virens. Phytopathology, 94, 171–176.
  • Harman G.E., 2000. Myths and dogmas of biocontrol. Changes in perceptions derived from research on Trichoderma harzianum T22. Plant Disease, 84, 377–393.
  • Harman G.E., Howell C.R., Viterbo A., Chet I., Lorito M., 2004. Trichoderma species: opportunistic, avirulent, plant symbionts. Nature Reviews Microbiology, 2, 43–56.
  • Howell C.R., 2002. Cotton seedling preemergence damping–off incited by Rhizopus oryzae and Pythium spp. and its biological control with Trichoderma spp. Phytopathology, 92, 177–180.
  • Kapat A., Panda T., 1997. pH and thermal stability studies of chitinase from Trichoderma harzianum: a thermodynamic consideration. Bioprocess Engineering, 16, 269–272.
  • Kapteyn J.C., Van den Ende H., Klis F.M., 1999. The contribution of cell wall proteins to the organization of the yeast cell wall. Biochimica et Biophysica Acta, 1426, 373–383.
  • Kubicek C.P., Mach R.L., Peterbauer C.K., Lorito M., 2001. Trichoderma: from genes to biocontrol. Journal of Plant Pathology, 83, 11–23.
  • Markovich N.A., Kononova G.L., 2003. Lytic enzymes of Trichoderma and their role in plant defense from fungal diseases: a review. Applied Biochemistry and Microbiology, 39, 341–351.
  • Metcalf D.A., Wilson C.R., 2001. The process of antagonism of Sclerotium cepivorum in white rot affected onion roots by Trichoderma koningii. Plant Pathology, 50, 249–257.
  • Michalik B., Biel W., Lubowicki R., Jacyno E., 2014. Chemical composition and biological value of proteins of the yeast Yarrowia lipolytica growing on industrial glycerol. Canadian Journal of Animal Science, 94, 99–104. doi:10.4141/CJAS2013-052
  • Noronha E.F., Kipnis A., Junqueira-Kipnis A.P., Ulhoa C.J., 2000. Regulation of 36-kDa β-1,3-glucanase synthesis in Trichoderma harzianum. FEMS Microbiology Letters, 188, 19–22.
  • Patil R.S., Ghormade V., Desphande M.V., 2000. Chitinolytic enzymes: an exploration. Enzyme and Microbial Technology, 26, 473–483.
  • Piegza M., Szlączka K., Łaba W., Witkowska D., 2014. Effect of carbon source on the production of lytic enzymes by filamentous fungi of the Trichoderma genus. EJPAU, 17(2), 06.
  • Rattanakit N., Plikomol A., Yano S., Wakayama M., Tachiki T., 2002. Utilization of shrimp shellfish waste as a substrate for solid-state cultivation of Aspergillus sp. S 1–13: Evaluation of a culture based on chitinase formation which is necessary for chitin–assimilation. Journal of Bioscience and Bioengineering, 93, 550–556.
  • Revah-Moiseev S., Carroad P.A., 1981. Conversion of the enzymatic hydrolysate of shellfish waste chitin to single-cell protein. Biotechnology & Bioengineering, 23, 1067–1078.
  • Vyas P.R., 1991. Studies on chitinolytic enzymes. Pune. University of Pune. Ph. D. thesis.
  • Vyas P.R., Deshpande M.V., 1991. Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP. The Journal of General and Applied Microbiology, 37, 267–275.
  • Witkowska D., Maj A., 2002. Production of lytic enzymes by Trichoderma sp. and their effect on the growth of phytopathogenic fungi. Folia Microbiologica, 47, 279–282.
  • Witkowska D., Stempniewicz R., Maj A., 1999. Lytic enzymes from Trichoderma and their utilization of yeast protoplast formation. Polish Journal of Food and Nutrition Sciences, 49, 245–252.
  • Witkowska D., Stempniewicz R., Wojtatowicz M., 1997. Production of lytic enzymes using Trichoderma reesei M7-1 in yeast protoplast formation. Polish Journal of Food and Nutrition Sciences, 6, 51–60.
  • Xiao Y., Morrell J.J., 2004. Production of protoplasts from cultures of Ophiostoma picea. Journal of Wood Science, 50, 445–449.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
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