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  • 1
    Publication Date: 2016-02-26
    Description: The fungal kingdom is the source of almost all industrial enzymes in use for lignocellulose bioprocessing. We developed a systems-level approach that integrates transcriptomic sequencing, proteomics, phenotype, and biochemical studies of relatively unexplored basal fungi. Anaerobic gut fungi isolated from herbivores produce a large array of biomass-degrading enzymes that synergistically degrade crude, untreated plant biomass and are competitive with optimized commercial preparations from Aspergillus and Trichoderma. Compared to these model platforms, gut fungal enzymes are unbiased in substrate preference due to a wealth of xylan-degrading enzymes. These enzymes are universally catabolite-repressed and are further regulated by a rich landscape of noncoding regulatory RNAs. Additionally, we identified several promising sequence-divergent enzyme candidates for lignocellulosic bioprocessing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Solomon, Kevin V -- Haitjema, Charles H -- Henske, John K -- Gilmore, Sean P -- Borges-Rivera, Diego -- Lipzen, Anna -- Brewer, Heather M -- Purvine, Samuel O -- Wright, Aaron T -- Theodorou, Michael K -- Grigoriev, Igor V -- Regev, Aviv -- Thompson, Dawn A -- O'Malley, Michelle A -- New York, N.Y. -- Science. 2016 Mar 11;351(6278):1192-5. doi: 10.1126/science.aad1431. Epub 2016 Feb 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, University of California, Santa Barbara (UCSB), Santa Barbara, CA 93106, USA. ; Broad Institute of MIT and Harvard, Cambridge, MA 02143, USA. ; U.S. Department of Energy (DOE) Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA. ; Earth and Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA. Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352, USA. ; Earth and Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA. ; Animal Production, Welfare and Veterinary Sciences, Harper Adams University, Newport, Shropshire TF10 8NB, UK. ; Department of Chemical Engineering, University of California, Santa Barbara (UCSB), Santa Barbara, CA 93106, USA. momalley@engineering.ucsb.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26912365" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspergillus/*enzymology/genetics/isolation & purification ; Biotechnology/*methods ; Cellulases/genetics/isolation & purification/*metabolism ; Cellulose/metabolism ; Gastrointestinal Tract/*microbiology ; Herbivory ; RNA, Untranslated/genetics ; Substrate Specificity ; Trichoderma/*enzymology/genetics/isolation & purification ; Xylans/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: It is widely believed that the initial degradation of proteins contained in grazed forage is mediated by rumen micro-organisms, but the authors’ recent work suggests that the plant cells themselves contribute to their own demise. In the present study the responses of Lolium perenne leaves to the rumen environment were investigated by using an in vitro system which simulates the main stresses of the rumen but from which rumen micro-organisms were excluded. Degradation of leaf protein and the accumulation of amino acids in tissue and bathing medium occurred over a time-scale that is relevant to rumen function, and in a near 1 : 1 ratio. Significant loss of nuclear material was observed after 6 h incubation and chloroplasts became morphologically more spherical as the incubation progressed. In situ localization suggested that ribulose 1,5 bisphosphate carboxylase/oxygenase was broken down within chloroplasts which from cytology were judged to be intact. We conclude from these data that plant metabolism may play a significant role in breaking down plant proteins within relatively intact organelles in the rumen. The determinations of chlorophyll content and cell viability revealed that the plant processes occurring in the simulated rumen were similar but not identical to those of natural senescence.
    Type of Medium: Electronic Resource
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