Cellulases: ambiguous nonhomologous enzymes in a genomic perspective.

نویسندگان

  • Leonid O Sukharnikov
  • Brian J Cantwell
  • Mircea Podar
  • Igor B Zhulin
چکیده

The key material for bioethanol production is cellulose, which is one of the main components of the plant cell wall. Enzymatic depolymerization of cellulose is an essential step in bioethanol production, and can be accomplished by fungal and bacterial cellulases. Most of the biochemically characterized bacterial cellulases come from only a few cellulose-degrading bacteria, thus limiting our knowledge of a range of cellulolytic activities that exist in nature. The recent explosion of genomic data offers a unique opportunity to search for novel cellulolytic activities; however, the absence of clear understanding of structural and functional features that are important for reliable computational identification of cellulases precludes their exploration in the genomic datasets. Here, we explore the diversity of cellulases and propose a genomic approach to overcome this bottleneck.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Defining cellulase in the glycosyl hydrolase family 48 1 Sequence, Structure, and Evolution of Cellulases in the Glycoside Hydrolase Family 48

Background: Cellulases are non-homologous isofunctional enzymes, which prevents their unambiguous identification in genomic datasets. Results: Cellulases from glycoside hydrolase family 48 have distinct evolutionarily conserved sequence and structural features. Conclusion: Conserved sequence/structure features can be used to differentiate cellulases from non-cellulases in genomic datasets. Sign...

متن کامل

Defining Cellulase in the Glycosyl Hydrolase Family 48 Sequence, Structure, and Evolution of Cellulases in the Glycoside Hydrolase Family 48

Background: Cellulases are non-homologous isofunctional enzymes, which prevents their unambiguous identification in genomic datasets. Results: Cellulases from glycoside hydrolase family 48 have distinct evolutionarily conserved sequence and structural features. Conclusion: Conserved sequence/structure features can be used to differentiate cellulases from non-cellulases in genomic datasets. Sign...

متن کامل

Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48.

Currently, the cost of cellulase enzymes remains a key economic impediment to commercialization of biofuels. Enzymes from glycoside hydrolase family 48 (GH48) are a critical component of numerous natural lignocellulose-degrading systems. Although computational mining of large genomic data sets is a promising new approach for identifying novel cellulolytic activities, current computational metho...

متن کامل

Genomics of Aerobic Cellulose Utilization Systems in Actinobacteria

Cellulose degrading enzymes have important functions in the biotechnology industry, including the production of biofuels from lignocellulosic biomass. Anaerobes including Clostridium species organize cellulases and other glycosyl hydrolases into large complexes known as cellulosomes. In contrast, aerobic actinobacteria utilize systems comprised of independently acting enzymes, often with carboh...

متن کامل

PRODUCTION, RELEASE AND THERMAL CHARACTERIZATION OF CELLULOLYTIC ENZYME FROM CELLULOMONAS sp. STRAIN "0"

Cellulase production by a Cellulomonas sp., isolated in 1985 from forest humus soil along the border of the Caspian Sea in Iran, was investigated. This strain secreted endo-and exo-cellulases in the culture medium, but some of the enzymes produced remained cell membrane bound. Cell bound enzymes were released by various treatments. The highest amount of endo-glucanase (up to 95%) and exo-gl...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Trends in biotechnology

دوره 29 10  شماره 

صفحات  -

تاریخ انتشار 2011