Purification and partial characterization of a cellodextrin glucohydrolase (β‐glucosidase) from <i>Trichoderma reesei</i> strain QM 9414

Schmid, Georg; Wandrey, C.

doi:10.1002/bit.260300415

Cited by 47 publications

(21 citation statements)

References 41 publications

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“…β-Glucosidase multiplicity has been reported in number of filamentous fungi and yeast. For instances, multiplicity of β-glucosidase has been demonstrated in T. reesei [170,171]. A. niger NII-08121/MTCC 7956 was found to express four β-glucosidase isoforms when grown on lactose or cellulose, whilst 2 isoforms were expressed on wheat bran or rice straw as carbon source [172].…”

Section: Multiplicity Of β-Glucosidasementioning

confidence: 99%

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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Cellulose is the most abundant biomaterial in the biosphere and the major component of plant biomass.Cellulase is an enzymatic system required for conversion of renewable cellulose biomass into free sugar for subsequent use in different applications. Cellulase system mainly consists of three individual enzymes namely: endoglucanase, exoglucanase and β-glucosidases. β-Glucosidases are ubiquitous enzymes found in all living organisms with great biological significance. β-Glucosidases have also tremendous biotechnological applications such as biofuel production, beverage industry, food industry, cassava detoxification and oligosaccharides synthesis. Microbial β-glucosidases are preferred for industrial uses because of robust activity and novel properties exhibited by them. This review aims at describing the various biochemical methods used for screening and evaluating β-glucosidases activity from microbial sources. Subsequently, it generally highlights techniques used for purification of β-glucosidases. It then elaborates various biochemical and molecular properties of this valuable enzyme such as pH and temperature optima, glucose tolerance, substrate specificity, molecular weight, and multiplicity. Furthermore, it describes molecular cloning and expression of bacterial, fungal and metagenomic β-glucosidases. Finally, it highlights the potential biotechnological applications of β-glucosidases.

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Section: Multiplicity Of β-Glucosidasementioning

confidence: 99%

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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“…Sternberg & Mandels (1980) proposed the existence of a constitutive and an inducible form of the enzyme in T. reesei. Based on an intensive purification procedure, Schmid & Wandrey (1987) demonstrated two distinct pglucosidases in the extracellular culture filtrates of T. reesei and the properties of one of the purified enzymes appears to be similar to the plasma-membrane-bound enzyme reported by Umile & Kubicek (1986). Recently, based on the similar M , and PI values of the membranebound enzyme and an extracellular p-glucosidase, Jackson & Talburt (1988) made similar conclusions.…”

Section: Discussionmentioning

confidence: 68%

“…Second, the major source of the extracellular enzyme may not be the wall-bound enzyme, believed to be released on autolysis of the mycelium (Vaheri et al, 1979a;Kubicek, 1981) but either the intracellular enzyme or the 'plasma-membranebound' enzyme. The multiplicity of p-glucosidases has been suggested by several authors (Sternberg & Mandels, 1980;Kubicek, 1987;Schmid & Wandrey, 1987;Jackson & Talburt, 1988) but the function of the various enzymes is still not clear. Sternberg & Mandels (1980) proposed the existence of a constitutive and an inducible form of the enzyme in T. reesei.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of a Mutant of Trichoderma reesei Showing Reduced Levels of Extracellular -Glucosidase

Mishra¹,

Rao²,

Deb³

1989

Microbiology

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A mutant (D6-1 3 ) of Trichoderma reesei that produced low levels of extracellular /?-glucosidase was physiologically and biochemically characterized. The mutant was unable to grow and produced very little cellulase activity on Solka-Floc, Avicel, micro-crystalline cellulose and acidswollen cellulose. Whereas growth was nearly normal on cellobiose, lactose and glucose, cellulase production was slightly decreased on cellobiose and lactose. The mutant produced nearly normal levels of FPA (filter-paper activity) and endoglucanase on sophorose. A distinct lag and a lowered specific sugar consumption rate was observed for the mutant on 0.3% cellobiose; this appeared to be due to lowered wall-bound /?-glucosidase activity. The multiplicity and role of different P-glucosidases in T. reesei is discussed. I N T R O D U C T I O NThe cellulase and /?-glucosidase systems from Trichoderma reesei have been extensively studied to understand the mechanism of cellulase induction by cellulose (Merivuori et al., 1984;Kubicek, 1987;Kubicek et al., 1988). The cellulase enzymes are inducible by cellulose, cellobiose, cellobionolactone, lactose and sophorose (Sternberg & Mandels, 1979Bruchmann et al., 1987), whereas glucose and glycerol are repressors of cellulase biosynthesis (Montenecourt & Eveleigh, 1979). Since cellulose is insoluble it has been suggested that the true inducer may be sophorose, resulting from the degradation of cellulose by the combined action of endoglucanase and P-glucosidase (Gritzali & Brown, 1979; Vaheri et al., 1979a,b). In T. reesei inhi bit ion of plasma-membrane-bound P-glucosidase by nojirimycin and glucono-b-lactone prevents endoglucanase induction by cello-oligosaccharides but not by sophorose, implicating /?-glucosidase in de novo cellulase induction (Kubicek, 1987).Direct evidence for the role of P-glucosidase in cellulase induction would be provided by the characteristics of T. reesei mutants negative for or low in /?-glucosidase production. This paper contains the first report of the isolation of a mutant of T. reesei low in extracellular /?-glucosidase production. The mutant was physiologically and biochemically characterized in terms of its ability to grow and to produce cellulases on insoluble and soluble cellulase inducers. The presence of P-glucosidases in other subcellular fractions was also investigated to understand the origin and multiplicity of the enzyme. METHODSOrganism and isolation of mutant. Trichoderma reesei D-1/6 (Ghose et al., 1982) was the parent strain. The low+ glucosidase mutant D6-13 used in this study was isolated as a routine auxotrophic mutant from D-1/6 using the UV-irradiation method described for isolation of amino acid auxotrophs in T. reesei by Toyama et al. (1984). The rate of survival of treated conidia was 1 %. D6-13 is a lysine-requiring auxotroph.

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“…For optimization process, cellobiose supposed to be a donor for transglycosylation reaction was not added in the reaction because glycosyl aesculin was still synthesized without cellobiose. It has been known that cellobiose has an inhibitory effect on most microbial β-glucosidase [11,21]. In this respect, the use of β-glucosidase without adding cellobiose will have a significant advantage for the enzymatic A B C Fig.…”

Section: Resultsmentioning

confidence: 99%

Optimization of Glycosyl Aesculin Synthesis by Thermotoga neapolitana β-Glucosidase Using Response-surface Methodology

Park¹,

Park²,

Cha³

2017

Journal of Life Science

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Glycosyl aesculin, a potent anti-inflammatory agent, was synthesized by transglycosylation reaction, catalyzed by Thermotoga neapolitana β-glucosidase, with aesculin as an acceptor. The key reaction parameters were optimized using response-surface methodology (RSM) and 2 μg of the enzyme. As shown by a statistical analysis, a second-order polynomial model fitted well to the data (p<0.05). The response surface curve for the interaction between aesculin and other parameters revealed that the aesculin concentration and reaction time were the primary factors that affected the yield of glycosyl aesculin. Among the tested factors, the optimum values for glycosyl aesculin production were as follows: aesculin concentration of 9.5 g/l, temperature of 84℃, reaction time of 81 min, and pH of 8.2. Under these conditions, 61.7% of glycosyl aesculin was obtained, with a predicted yield of 5.86 g/l.The maximum amount of glycosyl aesculin was 6.02 g/l. Good agreement between the predicted and experimental results confirmed the validity of the RSM. The optimization of reaction conditions by RSM resulted in a 1.6-fold increase in the production of glycosyl aesculin as compared to the yield before optimization. These results indicate that RSM can be effectively used for process optimization in the synthesis of a variety of biologically active glycosides using bacterial glycosidases.

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Purification and partial characterization of a cellodextrin glucohydrolase (β‐glucosidase) from Trichoderma reesei strain QM 9414

Cited by 47 publications

References 41 publications

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Isolation and Characterization of a Mutant of Trichoderma reesei Showing Reduced Levels of Extracellular -Glucosidase

Optimization of Glycosyl Aesculin Synthesis by Thermotoga neapolitana β-Glucosidase Using Response-surface Methodology

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