Indigo-binding Domains in Cellulase Molecules

نویسندگان

  • A. V. Gusakov
  • A. P. Sinitsyn
  • A. V. Markov
  • A. A. Skomarovsky
  • O. A. Sinitsyna
  • A. G. Berlin
  • N. V. Ankudimova
چکیده

Study of cellulase adsorption on indigo particles and insoluble cellulose, as well as experiments on indigo interaction with immobilized amino acids together with theoretical analysis of three-dimensional structures of enzyme molecules, provided an evidence that certain cellulases, which have hydrophobic domains (clusters of closely located aromatic and non-polar residues) on their surface, may bind significant amounts of indigo and thus act as emulsifiers helping the dye to float out of cellulose fibers to the bulk solution in the process of enzymatic denim treatment. Only those cellulases, which had such indigo-binding domains, could efficiently remove indigo from the denim fabric providing high abrasive effects on the surface of the material.

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

Nano Clay as New Tool for Discoloration of Deyed Denim Garmnet with Indigo

Until recently, discoloration of the denim garment has been carried out through various methods including mechanical, chemical, physical and enzymatic treatments. In this study, the nano clay was co-applied in bio stone washing of denim with cellulase to obtain denim garment with a new look and clear effluent. Acid and neutral cellulases along with nano clay were applied on the dyed denim fabri...

متن کامل

Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis.

Clostridium thermocellum is a well-characterized cellulose-degrading microorganism. The genome sequence of C. thermocellum encodes a number of proteins that contain type I dockerin domains, which implies that they are components of the cellulose-degrading apparatus, but display no significant sequence similarity to known plant cell wall-degrading enzymes. Here, we report the biochemical propert...

متن کامل

Molecular cloning of endo-beta-D-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae.

Three endoglucanase genes, designated the rce1, rce2, and rce3 genes, were isolated from Rhizopus oryzae as the first cellulase genes from the subdivision ZYGOMYCOTA: All the amino acid sequences deduced from the rce1, rce2, and rce3 genes consisted of three distinct domains: cellulose binding domains, linker domains, and catalytic domains belonging to glycosyl hydrolase family 45. The rce3 gen...

متن کامل

The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel.

A genomic library of Pseudomonas fluorescens subsp. cellulosa DNA, constructed in lambda ZAPII, was screened for carboxymethyl-cellulase activity. The pseudomonad insert from a recombinant phage which displayed elevated cellulase activity in comparison with other cellulase-positive clones present in the library, was excised into pBluescript SK- to generate the plasmid pC48. The nucleotide seque...

متن کامل

The Role of Cellulose Binding Domains in the Adsorption of Cellulases onto Fibers and Its Effect on the Enzymatic Beating of Bleached Kraft Pulp

The adsorption of cellulases onto fibers may be one of the most important factors affecting the enzymatic reaction between cellulases and fibers. This study investigated the adsorption kinetics involved, using isothermal adsorption equations. Cellulose binding domains (CBDs) were isolated from a commercial cellulase, and their role in the adsorption and enzymatic reaction was evaluated. Approxi...

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 2001