Biochemical characterization of an extracellular polygalacturonase from Trichoderma harzianum

Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>

“…The calculated molecular weight of the PGaseLg was approximately 39.0 kDa. This molecular mass is in agreement with previously reported PGase from other sources, such as Rhizomucorpusillus [18] and Tricodermaharzianum [32] (about 31 kDa), Acrophialophoranainiana (31 to 35.5 kDa) [14], Saccharomyces cerevisiae strain IM1-8b (36 kDa) [33], Neurosporacrassa (37 kDa) [23] or Rhizopusoryzae (37.44 kDa) [34]. Higher molecular mass PGase is known, such as from E. carotovora (43 kDa) [24] and A. giganteus (69.9 kDa) [35].…”

Biotechnological potential of alternative carbon sources for production of pectinases by Rhizopus microsporus var. rhizopodiformis

“…Other media also supported significant enzymatic yield. For example, potatodextrose liquid medium plus 0.1% citric pectin for Trichoderma harzianum (Mohamed et al, 2006), or Kebede medium for Kluyveromyces wickerhamii (Moyo et al, 2003). Pectinolytic enzyme production has been reported as carbon source dependents (Gummadi and Panda, 2003;Blandino et al, 2001), as well as pH (Malvessi and Silveira, 2004), and temperature, culture time, aeration, and other parameters (Souza et al, 2003).…”

“…rhizopodiformis produced PG, which exhibited an optimum temperature (65ºC) suitable for future biotechnological applications. Mohamed et al (2006), reported a T. harzianum PG with optimum temperature at 40ºC, which retained 30% of its activity at 60ºC. The optimum temperature for PG from Bacillus sp.…”

“…The enzymatic activity decreased 28, 39 and 51% after incubation for 90 min at 60, 65 and 70ºC, respectively. The thermal inactivation of the T. harzianum (Mohamed et al, 2006) PG was investigated by incubating the enzyme for 15, 30 and 60 min, at 10 to 100ºC in the absence of substrate. The PG from T. reesei was stable at 40 and 50ºC (Mohamed et al, 2003).…”

“…The first group is represented by pectin esterase (PE) and the second by polygalacturonase (PG) and pectin lyase (PL). PG (EC 3.2.1.15) is a depolymerizing pectinase that catalyzes the hydrolysis of α-(1,4) glycosidic bounds between the non-esterified galacturonic acid units (Mohamed et al, 2006). Pectate lyase (EC 4.2.2.2) and PL (EC 4.2.10.10) cleave α-1,4-glycosidic linkages by trans-elimination, which results in galacturonide with an unsaturated bond between C4 and C5 at the non-reducing end of the galacturonic acid formed.…”