TY - JOUR
T1 - Regulation of β-1,3-glucanase by carbon starvation in the mycoparasite Trichoderma harzianum
AU - Ramot, Ofir
AU - Cohen-Kupiec, Rachel
AU - Chet, Ilan
PY - 2000/4
Y1 - 2000/4
N2 - The β-1,3-glucanase system of the mycoparasitic T. harzianum, isolate T-Y, was found to be composed of at least five different enzymes. Their migration distance in acrylamide gels corresponded to peptides with molecular masses of 30-200 kDa, and they were named accordingly. The largest enzyme - Gβ-1,3-200, was the most abundant when T-Y was grown with no carbon source. Its secretion was almost eliminated when T-Y was grown on media containing a high concentration of carbon sources such as N-acetylglucosamine (GlcNAc) or malic acid. Several isolates of T. harzianum were found to have a β-1,3-glucanase secretion system, controlled by catabolite repression. Each isolate exhibited a different β-1,3-glucanase profile Gβ-1,3-200 was isolated and purified its molecular mass was approximately 75 kDa, and its activity was of the exo-type, specific to β-1,3-glucan linkages. Four short peptides resulting from proteolysis of this enzyme were sequenced, and their sequences were most homologous to LAM13, a previously isolated β-1,3-glucanase.
AB - The β-1,3-glucanase system of the mycoparasitic T. harzianum, isolate T-Y, was found to be composed of at least five different enzymes. Their migration distance in acrylamide gels corresponded to peptides with molecular masses of 30-200 kDa, and they were named accordingly. The largest enzyme - Gβ-1,3-200, was the most abundant when T-Y was grown with no carbon source. Its secretion was almost eliminated when T-Y was grown on media containing a high concentration of carbon sources such as N-acetylglucosamine (GlcNAc) or malic acid. Several isolates of T. harzianum were found to have a β-1,3-glucanase secretion system, controlled by catabolite repression. Each isolate exhibited a different β-1,3-glucanase profile Gβ-1,3-200 was isolated and purified its molecular mass was approximately 75 kDa, and its activity was of the exo-type, specific to β-1,3-glucan linkages. Four short peptides resulting from proteolysis of this enzyme were sequenced, and their sequences were most homologous to LAM13, a previously isolated β-1,3-glucanase.
UR - http://www.scopus.com/inward/record.url?scp=0034097821&partnerID=8YFLogxK
U2 - 10.1017/S0953756299001471
DO - 10.1017/S0953756299001471
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:0034097821
SN - 0953-7562
VL - 104
SP - 415
EP - 420
JO - Mycological Research
JF - Mycological Research
IS - 4
ER -