ArticleBiotechnology letters2017
Hydrolytic potential of five fungal supernatants to enhance a commercial enzyme cocktail.
Article in Biotechnology letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 31 citations in OpenAlex.
- Improving saccharification of ramie stalks by synergistic effect of in-house cellulolytic enzymes consortium.AMB Express · 2022Article
- Potential Fungi Isolated From Anti-biodegradable Chinese Medicine Residue to Degrade Lignocellulose.Frontiers in microbiology · 2022Article
- Harnessing microbial wealth for lignocellulose biomass valorization through secretomics: a review.Biotechnology for biofuels · 2021Review
- A screening approach for assessing lytic polysaccharide monooxygenase activity in fungal strains.Biotechnology for biofuels · 2019Article
- The influence of feedstock characteristics on enzyme production inBiotechnology for biofuels · 2019Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectivesTo evaluate the potential of enzyme cocktails produced by five filamentous fungi to supplement the industrial cellulase cocktail, Celluclast 1.5L, in order to improve the efficiency of saccharification.
resultsThe fungi were cultivated on wheat bran and the resulting supernatants were combined with Celluclast in enzymatic hydrolysis experiments to test their ability to hydrolyze wheat bran and five cellulose-rich substrates. The supernatant showing the best performance was that from an Aspergillus niger cellulase mutant. The addition of β-glucosidase only to the Celluclast cocktail was not as beneficial.
conclusionSupplementing commercial cocktails with enzymes from carefully selected fungi may result in significantly more efficient saccharification of lignocellulosic materials. Furthermore, such an approach could lead to the identification of novel enzyme activities crucial for saccharification.
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