Purification and properties

نویسندگان

  • Leon D. RUTTERSMITH
  • Roy M. DANIEL
چکیده

Exo-1,4-fl-cellobiohydrolase (EC 3.2.1.91) was isolated from the culture supernatant of Thermotoga sp. strain FjSS3-B.1, an extremely thermophilic eubacterium that grows optimally at 80 'C. The enzyme was purified to homogeneity as determined by SDS/PAGE and has an Mr of 36000. The enzyme is the most thermostable cellulase reported to date, with a half-life at 108 'C of 70 min in buffer. In a 40 min assay, maximal activity was recorded at 105 'C. Cellobiohydrolase from strain FjSS3-B.1 is active against amorphous cellulose and CM-cellulose but only effects limited hydrolysis of filter paper or Sigmacell 20. The only product identified by h.p.l.c. is the disaccharide cellobiose. The enzyme has a pH optimum around neutral and is stabilized by the presence of 0.8 M-NaCl.

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

خالص‌سازی آنزیم لاکاز قارچ Trametes و تعیین خصوصیات فیزیکوشیمیایی لاکاز نوترکیب: یک مطالعه آزمایشگاهی

Background and Objectives: Laccase is the most abundant member of protein family that catalyzes the oxidation of substituted phenols. Laccases are used as biocatalysts for decolorization and bleaching in dye industries, detoxification in environment, and juice clarification in food industries. The present study aimed at producing recombinant laccase, purifying with high yield and fold, and char...

متن کامل

Proteins Separation and Purification Methods with Focus on Chromatography: a Review Study

  Before describing the structure and mechanism of action of a protein, it must first be subject to purification procedure. Protein purification is a set of processes in which one or a small number of proteins are purified from a complex compound that may be a complete cell, tissue, or organism. Understanding the functions, structural properties, and interactions of the protein are directly re...

متن کامل

PURIFICATION AND PROPERTIES OF AN EXTRACELLULAR PROTEASE PRODUCED BY PENICIUIUM EXPANSUM

Penicilliurn expamum grown in a medium with rice husk as a carbon source produced an extracellular protease. The protease enzyme was isolated from culture broth by fractionation with acetone and column chromatography on Sephadex G- 100 and DEAE A-50. The protease enzyme was purified about 17.47 fold, with a recovery of 14%. The purified protease was homogenous on SDS polyacrylarnide disc ge...

متن کامل

PURIFICATION AND PROPERTIES OF RAT GASTROCNEMIUS MUSCLE N-ACETYL-I3-DGLUCOSAMINIDASE A AND B.

N-acetyl-B-D-Glucosaminidase was purified by affinity and ionexchange chromatography. Two major, A and B, and three minor intermediate forms were isolated and characterized. NAG-A and NAG-B were purified 440 and 1200 fold with final yields of 16 and 23 percent respectively. Each activity was represented by a single protein band. After 70 min preincubation at 55°C a loss of70% activity of N...

متن کامل

PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA

The first enzyme of the pathway for uridine diphosphate N-acetyl-D-glucosamine (UDPAG) biosynthesis i.e. L-glutamine: D-fructose 6-P amidotransferase (E.C. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on DEAE-Sephadex A-50. The enzyme showed optimal activity in a broad range of pH from 5.8 to 7.8 in both phosphate and cacodylate ...

متن کامل

Ziziphus mauritiana mediated synthesis of copper and nickel nanoparticles for comparative efficacy in biological water purification

The burden of life on the earth is the source of biological contamination in water. Nanotechnology has promising contributions in control of microbial contaminations and medicinal plants further increase these properties. Presently, copper acetate and nickel oxide nanoparticles were synthesized using 1mM solution of each with Ziziphus mauritiana leaves extract as reducing agent. Nanoparticles w...

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:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005