1988
DOI: 10.1007/bf00940165
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Production and stabilization of cellulases fromTrichoderma reesei

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Cited by 8 publications
(5 citation statements)
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“…Although this decrease in enzymatic activity is commonly observed during cellulase production, this phenomenon is not completely understood. Some authors have suggested that the decrease in activity may be due to the effects of a protease on the stability of the cellulases [32], but the presence of inhibitors may also interfere. However, the culture initiated with 0.75% sorbitol and supplemented with cellulose (0.75%) at 12 h after the start of cultivation (Sorb 0.75 + Cel 0.75 (12 h)) reached FPA values of 1.57 ± 0.27 IU.mL −1 .…”
Section: Resultsmentioning
confidence: 99%
“…Although this decrease in enzymatic activity is commonly observed during cellulase production, this phenomenon is not completely understood. Some authors have suggested that the decrease in activity may be due to the effects of a protease on the stability of the cellulases [32], but the presence of inhibitors may also interfere. However, the culture initiated with 0.75% sorbitol and supplemented with cellulose (0.75%) at 12 h after the start of cultivation (Sorb 0.75 + Cel 0.75 (12 h)) reached FPA values of 1.57 ± 0.27 IU.mL −1 .…”
Section: Resultsmentioning
confidence: 99%
“…Culture medium should have adequate levels of inducer, which can be the substrate, a substrate analogue or the product of the enzyme reaction (Rosenfeld and Feigelson 1969;Kurasawa et al 1992). Substrate analogues are more potent inducers than the substrate itself because they are not acted upon by the enzymes they induce; in the case of depolymerases, inducers are usually intermediate or end products of hydrolysis, since the substrate as such cannot enter the cell to trigger the mechanism (Illanes and Rossi 1981;Illanes et al 1988a). Level and time of addition of the inducer affects the level of enzyme synthesized and are operation parameters that should be optimized .…”
Section: Enzyme Synthesismentioning
confidence: 99%
“…Conditions that maximize the specific cell growth rate are often in compromise with those that maximize the specific rate of enzyme production (Gordillo et al 1998). In fact, it is usual that pH (Illanes et al 1988a;McDermid et al 1988), temperature (Akinrefon 1969;Feller et al 1994) and the level of dissolved oxygen (García-Garibay et al 1987; Barberis and Gentina 1998) optimal for growth differ from the corresponding optima for enzyme production. Compromise values are often used, but impressive increases in enzyme productivity have been reported by profiling these variables during cell culture (Mukhopadhyay and Malik 1980;Mukhopadhyay 1981;Ioniţȃ et al 2001).…”
Section: Enzyme Synthesismentioning
confidence: 99%
“…The rate and extent of cellulose conversion depends, among other things, on the amount of fl-glucosidase activity present in the cetlulase preparation used for efficient saccharification. The most studied fungal source of cellulase, ?>ichoderma reesei, (Illanes et al 1988;Panda 1989) has very little fi-glucosidase activity, which is a disadvantage from the point of view of efficient saccharification. The most studied fungal source of cellulase, ?>ichoderma reesei, (Illanes et al 1988;Panda 1989) has very little fi-glucosidase activity, which is a disadvantage from the point of view of efficient saccharification.…”
mentioning
confidence: 99%