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Efficient, Cost-Effective Laccase Enzymes for Industrial Manufacturing

标题

Archaeal Laccases and Multicopper Oxidases (MCOs) and Their uses thereof

详细技术说明

None

*Abstract

Invention

This recently discovered laccase enzyme has the potential for use in a broad array of industrialized processes, particularly wood pulp, paper, and fabric manufacturing. Researchers at the University of Florida have discovered a version of laccase in an organism that lives in extreme saline environments, such as the Dead Sea. Compared to other laccase enzymes, this new laccase enzyme has a higher catalytic rate and remains stable in harsh environmental conditions. This new Archaea-based laccase maintains catalytic activity at high temperature, extreme pH, or high salt conditions, making it a great candidate for a number of applications involving laccases. The researchers also discovered a simpler, more cost-effective enzymes extraction and purification procedure that offers high-efficiency yields for potential manufacturers, making the technology competitive on the market.

Application

High rate laccase enzyme that remains stable in harsh environmental conditions for use in industrial manufacturing, especially wood pulp, paper, and fabric manufacturing

Advantages

• Maintains stability during extreme heat, salt, and pH conditions, providing key advantage in many manufacturing processes
• Simplifies extraction and purification process, increasing the efficiency of manufacture yields
• Fits a broad range of applications, providing multiple market opportunities

Technology

The proposed technology is a highly thermostable, salt-tolerant laccase. Originally thought to be restricted to eukaryotes and bacteria, laccases have recently been discovered in Archaea—a group of organisms that often live in extreme environments. The ability of this newly discovered Archaeal laccase to maintain catalytic activity in the harshest of conditions makes it a perfect candidate for many industrial processes. Since the laccase produced by Haloferax volcanii purifies in an active form from extracellular medium and from recombinant E. coli without need for refolding, isolation of the enzyme is simpler and less expensive than that of many other laccases from other sources. This new enzyme improves performance in many applications that require higher temperatures or the use of solvents, opening up new applications for laccases and potentially providing a means to improve productivity of existing processes.

*IP Issue Date

Apr 9, 2013

*IP Publication Date

Apr 19, 2012

*Principal Investigation

Name: Julie A Maupin

Department:

Name: Boutaiba Saad

Department:

Name: Matthew Humbard

Department:

Name: Sivakumar Uthandi

Department:

附加资料

Inventor: Maupin-Furlow, Julie A. | Uthandi, Sivakumar | Saad, Boutaiba | Humbard, Matthew A.
Priority Number: US8414660B2
IPC Current: C09B006700 | C02F000100 | C08H000700 | C12N000902
US Class: 008401 | 210632 | 435189 | 527400
Assignee Applicant: University of Florida Research Foundation Inc.inesville
Title: Haloferax volcanii laccase and variants and fragments thereof
Usefulness: Haloferax volcanii laccase and variants and fragments thereof
Summary: For oxidizing a phenolic substrate, for oxidizing bilirubin to biliverdin and water and for bleaching dye, bleaching pulp for paper production, for modifying lignin, for the treatment of waste water, for delignification and/or detoxification of acid-pretreated biomass; and used in genetically engineered host cell (claimed).
Novelty: New purified polypeptide with laccase activity obtained from Haloferax volcanii useful e.g. for oxidizing a phenolic substrate, for oxidizing bilirubin and for bleaching dye, for the treatment of waste water and for modifying lignin

主要类别

环保/绿色科技

细分类别

废液处理

申请日期

Jan 4, 2012

申请号码

8,414,660

其他

国家/地区

美国