Production of beta-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: partial purification of two isozymes.
Trichoderma reesei FTKO-39 grown at 35 degrees C for 5 d on wheat bran supplemented with MgCl2 and lactose as the carbon source produced two isozymes of beta-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimum activity at 65 degrees C, but the pH optima were 4.0 and 6.5, respectively. The isozymes also showed similar thermal stability. However, BGT I was more stable than BGT II in a pH range of 3.0-10.0. At least two different beta-galactosidases are produced by T. reesei, as revealed by the two bands seen on a 6% polyacrylamide gel stained for activity.
Adalberto
P R
PR
Department of General Inorganic and Chemistry, Institute of Chemistry, Rua Prof. Francisco Degni, s/n, 14800-900, Araraquara, SP, Brazil.
Massabni
A C
AC
Goulart
A J
AJ
Contiero
J
J
Carmona
E C
EC
Cardello
L
L
Monti
R
R
D004043:Dietary Fiber / Q000378:metabolism* / Q000382:microbiology*; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D007700:Kinetics; D014242:Trichoderma / Q000201:enzymology*; D014908:Triticum / Q000201:enzymology / Q000382:microbiology*; D001616:beta-Galactosidase / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification*
D004043:Dietary Fiber; D007527:Isoenzymes; D001616:beta-Galactosidase