Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Cellobiohydrolase from Trichoderma reesei.

M Nummi, M L Niku-Paavola, A Lappalainen

    The Biochemical Journal
    |December 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Co-infections with respiratory viruses in dogs with bacterial pneumonia.

    Journal of veterinary internal medicine·2015
    Same author

    Spina bifida occulta and enuresis.

    Zeitschrift fur Kinderpsychiatrie. Revue de psychiatrie infantile·2014
    Same author

    Enzymatic hydrolysis of cellulose: is the current theory of the mechanisms of hydrolysis valid?

    Critical reviews in biotechnology·2010
    Same author

    Quantitative magnetic resonance imaging of experimentally injured porcine intervertebral disc.

    Acta radiologica (Stockholm, Sweden : 1987)·2007
    Same author

    Calcification of the intervertebral discs and curvature of the radius and ulna: a radiographic survey of Finnish miniature dachshunds.

    Acta veterinaria Scandinavica·2001
    Same author

    Endoxylanase II from Trichoderma reesei has several isoforms with different isoelectric points.

    Biotechnology and applied biochemistry·2000
    Same journal

    Mechanistic insights into acetylated histone recognition by the CECR2 bromodomain.

    The Biochemical journal·2026
    Same journal

    Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

    The Biochemical journal·2026
    Same journal

    Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

    The Biochemical journal·2026
    Same journal

    Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

    The Biochemical journal·2026
    Same journal

    Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

    The Biochemical journal·2026
    Same journal

    A molecular perspective on dimethylarginine dimethylaminohydrolases structure and function.

    The Biochemical journal·2026
    See all related articles

    Researchers purified a highly effective 1,4-beta-D-glucan cellobiohydrolase enzyme from Trichoderma reesei. This enzyme shows superior cellulose hydrolysis capabilities compared to previously studied enzymes.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Microbiology

    Background:

    • Cellobiohydrolases are crucial enzymes for cellulose degradation.
    • Trichoderma reesei is a well-known producer of industrial enzymes.
    • Efficient purification methods are essential for characterizing enzyme function.

    Purpose of the Study:

    • To purify and characterize a specific 1,4-beta-D-glucan cellobiohydrolase from Trichoderma reesei.
    • To assess the enzyme's effectiveness in cellulose hydrolysis.
    • To compare its properties with previously identified cellobiohydrolases.

    Main Methods:

    • Biospecific sorption on amorphous cellulose.
    • Immunoaffinity chromatography for enzyme purification.
    • Polyacrylamide-gel electrophoresis and immunoelectrophoresis for purity assessment.

    Related Experiment Videos

  • Determination of molecular weight (Mr) and isoelectric point (pI).

    • Main Results:

    • A single, active protein band/arc confirmed enzyme purity.
    • The purified enzyme had a molecular weight of 65,000 and pI of 4.2-3.6.
    • The enzyme contained approximately 10% hexose.
    • Demonstrated enhanced effectiveness in cellulose hydrolysis compared to known enzymes.

    Conclusions:

    • A highly pure and effective 1,4-beta-D-glucan cellobiohydrolase was isolated from Trichoderma reesei.
    • The characterized enzyme exhibits superior cellulose hydrolysis activity.
    • This enzyme represents a promising candidate for biotechnological applications in biomass conversion.