RETRACTED: Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production

Singhania, Reeta Rani; Patel, Anil Kumar; Sukumaran, Rajeev K.; Larroche, Christian; Pandey, Ashok

doi:10.1016/j.biortech.2012.09.012

Cited by 528 publications

(334 citation statements)

References 70 publications

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“…As commercial T. reesei cellulase preparations are typically low in β-glucosidase activity, supplementing with exogenous β-glucosidases, either by homologous or heterologous expression of β-glucosidase genes, or co-cultivating T. reesei with other high β-glucosidase-producing fungi, is often required for efficient hydrolysis of complex substrates [54]. Consequently, the relatively high proportion of β-glucosidases that we find in the T. asperellum enzyme blend (ID 4405, 15011, 4404) could make it suitable to meet this requirement [10].…”

Section: Secretome Comparisonmentioning

confidence: 99%

On-Site Enzyme Production by Trichoderma asperellum for the Degradation of Duckweed

Bech¹,

Herbst²

2015

Fungal Genom Biol

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The on-site production of cell wall degrading enzymes is an important strategy for the development of sustainable bio-refinery processes. This study concerns the optimization of production of plant cell wall-degrading enzymes produced by Trichoderma asperellum. A comparative secretome analysis was performed on T. asperellum growing on PDA agar, wheat bran and duckweed, respectively. T. asperellum proved to be able to produce a wide enzyme profile, including both depolymerization and debranching enzymes, mainly consisting of hemi-cellulases. The secretome analysis showed specific glycoside hydrolase-induction on duckweed compared with growth on wheat bran and PDA, including a GH62 α-L-arabinofuranosidase, a promising candidate enzyme for the degradation of duckweed. The enzyme cocktail from T. asperellum proved capable of degrading pretreated duckweed, obtaining up to 60% of the theoretical glucose yield, making it a potential candidate for on-site enzyme production.

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Section: Secretome Comparisonmentioning

confidence: 99%

On-Site Enzyme Production by Trichoderma asperellum for the Degradation of Duckweed

Bech¹,

Herbst²

2015

Fungal Genom Biol

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“…Enzyme activity of culture supernatant that was done by using p-NPG (4-nitrophenyl β-Dglucopyranocide) as substrate was performed to determine the ability of cells to produce extracellular β-glucosidase enzymes. Artificial substrate of p-NPG was usually used to determine the β-glucosidase enzyme activity (Singhania et al, 2012). Cell protein extract samples were used to determine intracellular β-glucosidase enzyme activity.…”

Section: β-Glucosidasementioning

confidence: 99%

Extracellular β-Glucosidase Production from bglp15.2 Gene Carrying Inulinase Signal Peptide in Saccharomyces cerevisiae BY4741

Fitri¹,

Restiawaty

Moeis³

2017

Jurnal Biodjati

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One of the important enzymes in cellulase complex is β-glucosidase. In this research, adding signal peptide of inulinase gene from Kluyveromyces marxianus, cloning, and expressing of bglp15.2 gene in S. cerevisiae BY4741 had been done. Gene of bglp15.2 encoding β-glucosidase has 90% identity to nucleotide sequence of Shewanella frigidimarina NCIMB 400 bacteria. Adding nucleotide sequence of signal peptide was aimed to secrete β-glucosidase and had been done with PCR (Polymerase Chain Reaction) method. The addition of nucleotide sequence of signal peptide in bglp15.2 gene had been done succesfully that indicated from nucleotide sequencing result and the increment of amplicon band size in electroferogram of the last addition PCR step. The bglp15.2 and bglp15.2INU gene (the bglp15.2 gene that has signal peptide nucleotide sequence) were cloned in Escherichia coli DH5α using pGEM-T-Easy vector and pBEVY-GL shuttle vector. The pBEVY-GL shuttle vector was used for transforming S. cerevisiae BY4741 with bglp15.2 and bglp15.2INU. The recombinant S. cerevisiae BY4741 carrying bglp15.2INU gene and growing in 48 hours had extracellularly β-glucosidase enzyme activity of 0,0178 U/ml and the intracellularly activity was 0,0181 U/ml. The β-glucosidase enzyme without signal peptide was not secreted. With K. marxianus inulinase signal peptide, about 50% Bglp15.2INU protein could be secreted. The protein molecular weight of secreted Bglp15.2INU was 44 kDa in SDS-PAGE result.

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“…With the development of knowledge and technique, enzymes are involved in a more wide variety of applications such as food industries, textiles industries, chemical manufacture and other important industries [1]. However, there are some drawback for the use of enzyme such as the problem of purification and continuous operation, the lack of long-term stability and the difficulty in their recovery and reuse.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of glucoamylase on stimuli-sensitive macroporous semi-interpenetrating stimuli-sensitive hydrogel carriers

Li¹,

Yang²,

Zhu³

et al. 2017

2nd Annual International Conference on Energy, Environmental &Amp; Sustainable Ecosystem Development (EESED 2016)

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Based on the special phase transition property of copolymer hydrogel of N-is opropylacrylamide, the immobilization of glucoamylase on five macro porous semi-interpenetrating stimuli-sensitive hydrogel carriers was studied. Four good preparations were screened, i.e. GelNIPAm/PAEMA-2.5, Gel NAEP/PAEMA-2.5, Gel NAP/PAEMA-2.5 and Gel NDEP/PAEMA-2.5, the immobilization yield °C activity) of them were 11.4%, 12.7%, 14.9% and 15.3% respectively under optimal conditions. The most preferred temperature of these immobilized glucoamylase was 30 °C , and the adapted pH was about pH 4.5. The activities of the latter three photo-sensitive preparations could be adjusted by UV irradiation during their phase transition. After month storage, the activity retention rate was no less than 80% for every one preparations cross-linked with 2.5 vol % of glutaraldehyde.

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RETRACTED: Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production

Cited by 528 publications

References 70 publications

On-Site Enzyme Production by Trichoderma asperellum for the Degradation of Duckweed

On-Site Enzyme Production by Trichoderma asperellum for the Degradation of Duckweed

Extracellular β-Glucosidase Production from bglp15.2 Gene Carrying Inulinase Signal Peptide in Saccharomyces cerevisiae BY4741

Immobilization of glucoamylase on stimuli-sensitive macroporous semi-interpenetrating stimuli-sensitive hydrogel carriers

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