New monolithic enzymatic micro-reactor for the fast production and purification of oligogalacturonides

被引:30
作者
Delattre, C. [1 ]
Michaud, P. [2 ]
Vijayalakshmi, M. A. [1 ]
机构
[1] Univ Vellore, Vellore Inst Technol, Ctr BioSeparat Technol, Vellore 632014, Tamil Nadu, India
[2] Univ Blaise Pascal, Polytech Clermont Ferrand, Lab Genie Chim & Biochim, F-63174 Aubiere, France
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2008年 / 861卷 / 02期
关键词
CIM-disk; enzymatic bioreactor; monolith chromatography; oligouronides; pectin lyase;
D O I
10.1016/j.jchromb.2007.08.036
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Fast production and purification of alpha-(1,4)-oligogalacturonides was investigated using a new enzymatic reactor composed of a monolithic matrix. Pectin lyase from Aspergillus japonicus (Sigma) was immobilized on CIM-disk epoxy monolith. Studies were performed on free pectin lyase and immobilized pectin lyase to compare the optimum temperature, optimum pH, and thermal stability. It was determined that optimum temperature for free pectin lyase and immobilized pectin lyase on monolithic support is 30C, and optimum pH is 5. Monolithic CIM-disk chromatography is one of the fastest liquid chromatographic method used for separation and purification of biomolecules due to high mass transfer rate. In this context, online one step production and purification of oligogalacturonides was investigated associating CIM-disk pectin lyase and CIM-disk DEAE. This efficient enzymatic bioreactor production of uronic oligosaccharides from polygalacturonic acid (PGA) constitutes an original fast process to generate bioactive oligouronides. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:203 / 208
页数:6
相关论文
共 28 条
[11]   Oligogalacturonic acid and chitosan reduce stomatal aperture by inducing the evolution of reactive oxygen species from guard cells of tomato and Commelina communis [J].
Lee, S ;
Choi, H ;
Suh, S ;
Doo, IS ;
Oh, KY ;
Choi, EJ ;
Taylor, ATS ;
Low, PS ;
Lee, Y .
PLANT PHYSIOLOGY, 1999, 121 (01) :147-152
[12]   IMMOBILIZATION OF ENDO-POLYGALACTURONASE FROM ASPERGILLUS-NIGER ON VARIOUS TYPES OF MACROMOLECULAR SUPPORTS [J].
PIFFERI, PG ;
TRAMONTINI, M ;
MALACARNE, A .
BIOTECHNOLOGY AND BIOENGINEERING, 1989, 33 (10) :1258-1266
[13]  
Podgornik A, 1998, PROGR BIOTECHNOL, V15, P541
[14]   Characteristics of LiP immobilized to CIM monolithic supports [J].
Podgornik, H ;
Podgornik, A .
ENZYME AND MICROBIAL TECHNOLOGY, 2002, 31 (06) :855-861
[15]   Pectins: structure, biosynthesis, and oligogalacturonide-related signaling [J].
Ridley, BL ;
O'Neill, MA ;
Mohnen, DA .
PHYTOCHEMISTRY, 2001, 57 (06) :929-967
[16]  
Rombouts FM, 1980, MICROBIAL ENZYMES BI, P227
[17]   The use of commercial pectinase in the fruit juice industry, part 2: Determination of the kinetic behaviour of immobilized commercial pectinase [J].
Sarioglu, K ;
Demir, N ;
Acar, J ;
Mutlu, M .
JOURNAL OF FOOD ENGINEERING, 2001, 47 (04) :271-274
[18]   Application of compact porous disks for fast separations of biopolymers and in-process control in biotechnology [J].
Strancar, A ;
Koselj, P ;
Schwinn, H ;
Josic, D .
ANALYTICAL CHEMISTRY, 1996, 68 (19) :3483-3488
[19]  
Strancar A., 1998, LC GC, V11, P660
[20]   Short monolithic beds: history and introduction to the field [J].
Tennikova, TB ;
Reusch, J .
JOURNAL OF CHROMATOGRAPHY A, 2005, 1065 (01) :13-17