Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Treatment of cellulosic material and enzymes useful thererin

a cellulosic material and enzyme technology, applied in the field of cellulosic material production of sugar hydrolysates, can solve the problems of high bioethanol production cost, low energy output, and insatiable technology

Inactive Publication Date: 2009-02-12
ROAL O Y (FI)
View PDF14 Cites 78 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0022]It has now surprisingly been found that cellulolytic enzymes, and especially cellobiohydrolases obtainable from Thermoascus aurantiacus, Acremonium thermophilum, or Chaetomium thermophilum are particularly useful in hydrolyzing cellulosic material. In addition to cellobiohydrolases these fungi also have endoglucanases, beta-glucosidases and xylanases that are very suitable for degrading cellulosic material. The enzymes are kinetically very effective over a broad range of temperatures, and although they have high activity at high temperatures, they are also very efficient at standard hydrolysis temperatures. This makes them extremely well suited for varying cellulosic substrate hydrolysis processes carried out both at conventional temperatures and at elevated temperatures.

Problems solved by technology

Bioethanol production costs are high and the energy output is low, and there is continuous research for making the process more economical.
However, enzymatic hydrolysis is used only to a limited amount at industrial scale, and especially when using strongly lignified material such as wood or agricultural waste the technology is not satisfactory.
The cost of the enzymatic step is one of the major economical factors of the process.
Cellobiose conversion to glucose is usually the major rate-limiting step.
However, the majority of cellulases from less known fungi have not been applied in processes of practical importance such as in degrading cellulosic material, including lignocellulose.
This approach may lead to significant saving in energy and investments costs.
The high temperature also decreases the risk of contamination during hydrolysis.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Treatment of cellulosic material and enzymes useful thererin
  • Treatment of cellulosic material and enzymes useful thererin
  • Treatment of cellulosic material and enzymes useful thererin

Examples

Experimental program
Comparison scheme
Effect test

example 1

Screening for Strains Expressing Cellulolytic Activity and their Cultivation for Purification

[0104]About 25 fungal strains from the Roal Oy culture collection were tested for cellulolytic activity including beta-glucosidases. After preliminary screening six strains were chosen for further studies. These were Thermoascus aurantiacus ALKO4239 and ALKO4242, Acremonium thermophilum ALKO4245, Talaromyces thermophilus ALKO4246 and Chaetomium thermophilum ALKO4261 and ALKO4265.

[0105]The strains ALKO4239, ALKO4242 and ALKO4246 were cultivated in shake flasks at 42° C. for 7 d in the medium 3×B, which contains g / litre: Solka Floc cellulose 18, distiller's spent grain 18, oats spelt xylan 9, CaCO3 2, soybean meal 4.5, (NH4)HPO4 4.5, wheat bran 3.0, KH2PO4 1.5, MgSO4.H2O 1.5, NaCl 0.5, KNO3 0.9, locust bean gum 9.0, trace element solution #1 0.5, trace element solution #2 0.5 and Struktol (Stow, Ohio, USA) antifoam 0.5 ml; the pH was adjusted to 6.5. Trace element solution #1 has g / litre: MnSO...

example 2

Purification and Characterization of Cellobiohydrolases from Acremonium thermophilum ALKO4245 and Chaetomium thermophilum ALKO4265

[0122]Acremonium thermophilum ALKO4245 and Chaetomium thermophilum ALKO4265 were grown as described in Example 1. The main cellobiohydrolases were purified using p-aminobenzyl 1-thio-β-cellobioside-based affinity column, prepared as described by Tomme et al., 1988.

[0123]The culture supernatants were first buffered into 50 mM sodium acetate buffer pH 5.0, containing 1 mM δ-gluconolactone and 0.1 M glucose in order to retard ligand hydrolysis in the presence of β-glucosidases. Cellobiohydrolases were eluted with 0.1 M lactose and finally purified by gel filtration chromatography using Superdex 200 HR 10 / 30 columns in the ÄKTA system (Amersham Pharmacia Biotech). The buffer used in gel filtration was 50 mM sodium phosphate pH 7.0, containing 0.15 M sodium chloride.

[0124]Purified cellobiohydrolases were analysed by SDS-polyacrylamide gel electrophoresis and t...

example 3

Purification and Characterization of an Endoglucanase from Acremonium thermophilum ALKO4245

[0128]Acremonium thermophilum ALKO4245 was grown as described in Example 1. The culture supernatant was incubated at 70° C. for 24 hours after which it was concentrated by ultrafiltration. The pure endoglucanase was obtained by sequential purification with hydrophobic interaction and cation exchange chromatography followed by gel filtration. The endoglucanase activity of the fractions collected during purification was determined using carboxymethyl cellulose (CMC) as substrate (procedure of IUPAC 1987). Protein content was measured by BioRad Assay Kit (Bio-Rad Laboratories) using bovine serum albumine as standard.

[0129]The concentrated culture supernatant was applied to a HiPrep 16 / 10 Butyl FF hydrophobic interaction column equilibrated with 20 mM potassium phosphate buffer pH 6.0, containing 1 M (NH4)2SO4. Bound proteins were eluted with the linear gradient from the above buffer to 5 mM potas...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The present invention relates to the production of sugar hydrolysates from cellulosic material. The method may be used e.g. for producing fermentable sugars for the production of bioethanol from lignocellulosic material. Cellulolytic enzymes and their production by recombinant technology is described, as well as uses of the enzymes and enzyme preparations.

Description

RELATED APPLICATIONS[0001]This application is a continuation of PCT application no. PCT / FI2006 / 050558, designating the United States and filed Dec. 15, 2006; which claims the benefit of the filing date of Finnish application no. 20051318, filed Dec. 22, 2005; and U.S. application No. 60 / 753,258, filed Dec. 22, 2005; each of which is hereby incorporated herein by reference in its entirety for all purposes.FIELD[0002]The present invention relates to the production of sugar hydrolysates from cellulosic material. More precisely the invention relates to production of fermentable sugars from lignocellulosic material by enzymatic conversion. The fermentable sugars are useful e.g. in the production of bioethanol, or for other purposes. In particular the invention is directed to a method for treating cellulosic material with cellobiohydrolase, endoglucanase, beta-glucosidase, and optionally xylanase, and to enzyme preparations and the uses thereof. The invention is further directed to novel ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(United States)
IPC IPC(8): C12P7/10C12N9/42C07H21/00C12N15/64C12N1/21C12N1/20
CPCC12P7/10C12P19/02Y02E50/16Y02E50/17C12N9/96C12Y302/01091C12N9/2437C12N9/2445C12Y302/01004C12Y302/01021Y02E50/10C12N15/52C12N15/79Y02P20/52
Inventor VEHMAANPERA, JARIALAPURANEN, MARIKAPURANEN, TERHISIIKA-AHO, MATTIKALLIO, JARNOHOOMAN, SATUVOUTILAINEN, SANNIHALONEN, TEEMUVIIKARI, LIISA
Owner ROAL O Y (FI)
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com