Biodegradation of wastepaper by cellulase from Trichoderma viride

Wyk, J.P.H. van; Mohulatsi, M.

doi:10.1016/s0960-8524(02)00130-x

Cited by 69 publications

(29 citation statements)

References 8 publications

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“…It is known that cellulose is degraded by various cellulases including cellulase of white-rot fungi, Trichoderma reesei and Trichoderma viride. [7,8] For the plastic coated papers, these enzymes preferentially degraded cellulose at the points of uncoated fibers. However, these cellulases did not degrade PLA, PCL, PHB and PBS plastic powder.…”

Section: Resultsmentioning

confidence: 99%

A New Method for the Evaluation of Biodegradable Plastic Using Coated Cellulose Paper

Lim

Raku

Tokiwa

2004

Macromolecular Bioscience

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A highly sensitive analytical method for evaluation of poly(L-lactide) (PLA), poly(epsilon-caprolactone) (PCL), poly(beta-hydroxybutyrate) (PHB), and poly(butylene succinate) (PBS) degradability was developed using coated cellulose paper, prepared by penetration and adhesion of these plastics into/onto the cellulose paper. Enzymatic degradability of the obtained plastic coated papers was evaluated using various commercial proteases and lipases. PLA coated paper was highly susceptible to subtilisin and mammalian enzymes, alpha-chymotrypsin, elastase and trypsin. To our knowledge, this is the first report on the degradation of PLA coated paper using subtilisin and mammalian enzymes. Almost all lipase preparations degraded PCL and PHB coated papers but not PBS coated paper. The biodegradability of plastic coated paper was greater than that of plastic powder. The penetration of plastic into cellulose paper by coating improved the plastic degradability, and can be regulated easily.

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Section: Resultsmentioning

confidence: 99%

A New Method for the Evaluation of Biodegradable Plastic Using Coated Cellulose Paper

Lim

Raku

Tokiwa

2004

Macromolecular Bioscience

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“…In industry, these enzymes have found novel applications in the production of fermentable sugars and ethanol (Van Wyk, Mohulatsi, 2003), organic acids (Luo et al, 1997), detergents and other chemicals (Oksanen et al, 1998). They have been used in the pulp and paper industry, e. g., in deinking of fiber surfaces and in improving pulp drainage (Suurnäkki et al, 2004), in the textile industry (Miettinen-Oinonen et al, 2004), animal feed (Ishikuro, 1993), and even in the food industry (Penttilä et al, 2004), for the processing of paper and cellophane, as well as for biotransformation of waste cellulose to fermentable sugars (Van Wyk, Mohulatsi, 2003). The demand for more thermostable, highly active and specific cellulases is on the increase.…”

Section: Screening Of Endophytic Fungimentioning

confidence: 99%

Production of Cellulolytic Enzymes by Endophytic Fungi Isolated from Cameroonian Medicinal Plants

Toghueo¹,

Ejiya²,

Sahal³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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“…To study the transcriptional response of T. viride AS3.3711 egVIII to various substrates, 5 ml of a suspension of spores was inoculated into 50 ml MENDELS medium [15] (carbon source 10 g/L, (NH 4 ) 2 SO 4 Total RNA (10 μg) was extracted from mycelia of T. viride AS3.3711 using Trizol reagent (Invitrogen, Madison, WI, USA), separated on a 1.2% agarose gel containing 1.5% formaldehyde and blotted onto a Nylon membrane. Digoxigenin High Prime DNA Labeling and Detection Starter Kit II (Roche, Germany) were used for the probe preparation and transcript detection of the egVIII gene.…”

Section: Response Of Egviii In T Viride To Different Substratesmentioning

confidence: 99%

Cloning and Heterologous Expression of a Novel Endoglucanase Gene egVIII from Trichoderma viride in Saccharomyces cerevisiae

Huang

Yang

Liu

et al. 2009

Appl Biochem Biotechnol

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Endoglucanase is a major cellulolytic enzyme produced by the fungus Trichoderma viride. The 1,317 bp cDNA of endoglucanase gene egVIII was cloned from T. viride AS3.3711, encoding a 438 amino acid protein with a calculated molecular mass of 46.86 kDa and isoelectric point of 4.32. Sequence analysis suggested that EGVIII belonged to the glycosyl hydrolase family 5. The N-terminal region of EGVIII contains a signal peptide sequence of 19 amino acid residues, indicating that it is an extracellular enzyme. Transcription of the egVIII gene in T. viride AS3.3711 can be induced by carboxymethyl cellulose sodium (CMC-Na), sucrose, microcrystalline cellulose, and corn stalk, and inhibited by glucose and fructose. The alpha-mating factor signal can effectively enhance the secretion of the recombinant EGVIII in Saccharomyces cerevisiae, as demonstrated by the enzymatic activity of recombinant yeast IpYEMalpha-xegVIII in the supernatant, which was 0.86 times higher than that of the IpYES2-egVIII. Recombinant endoglucanase EGVIII showed optimal activity at a temperature of 60 degrees C and pH of 6.0. It was stable when incubated from 35 degrees C to 70 degrees C for 1 h. The enzymatic activity of recombinant EGVIII was stable at a pH 3.0 to 7.5 at 50 degrees C and reached the highest level at 0.174U when activated by 75 mM of Zn(2+). The Michaelis-Menten constant (Km) and Kcat values for CMC-Na and cellotriose hydrolysis were 3.82 mg/ml, 9.56 s(-1) and 1.75 mg/ml, 7.08 s(-1), respectively. Transgenic yeast strain IpYEMalpha-xegVIII might be useful for renewable fuels industries.

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Biodegradation of wastepaper by cellulase from Trichoderma viride

Cited by 69 publications

References 8 publications

A New Method for the Evaluation of Biodegradable Plastic Using Coated Cellulose Paper

A New Method for the Evaluation of Biodegradable Plastic Using Coated Cellulose Paper

Production of Cellulolytic Enzymes by Endophytic Fungi Isolated from Cameroonian Medicinal Plants

Cloning and Heterologous Expression of a Novel Endoglucanase Gene egVIII from Trichoderma viride in Saccharomyces cerevisiae

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