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- W2154207782 abstract "Significance Plant biomass decomposition has broad implications for the global carbon cycle, agriculture, and ecology, and it is primarily accomplished by fungi. Recently, research into fungal biomass degradation mechanisms has been driven by the growing biofuels industry, because enzymes from fungi are among the primary catalysts being investigated for industrial processes to convert polysaccharides into upgradeable sugars. Understanding the mechanisms used by polysaccharide-degrading enzymes and identifying means to improve their performance is of paramount importance because of the scale of enzyme production for biofuels processes. Here, we use glycoprotein synthesis and biophysical measurements to characterize the specific effects of glycosylation on ubiquitous fungal carbohydrate-binding modules for biomass degradation, which reveal key features of the importance of posttranslational modifications on enzyme function." @default.
- W2154207782 created "2016-06-24" @default.
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- W2154207782 date "2014-05-12" @default.
- W2154207782 modified "2023-10-12" @default.
- W2154207782 title "Specificity of <i>O</i> -glycosylation in enhancing the stability and cellulose binding affinity of Family 1 carbohydrate-binding modules" @default.
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- W2154207782 doi "https://doi.org/10.1073/pnas.1402518111" @default.
- W2154207782 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4040550" @default.
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