Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing compound containing saccharide radical
Patent
1994-08-12
1999-08-03
Marx, Irene
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing compound containing saccharide radical
435200, C12P 1902
Patent
active
059324520
DESCRIPTION:
BRIEF SUMMARY
The invention relates to a process for the hydrolysis of a hemicellulose substrate containing xylo-oligomers by hemicellulolytic enzymes immobilized by adsorbing on a solid carrier. The invention further concerns a combination of a solid carrier and a hemicellulolytic enzyme or mixture of enzymes immobilized on the carrier for realizing this process of hydrolysis. The process is well suited for the production of xylose from xylo-oligomers containing spent liquors of cellulose industries and from the water extracts of steam-exploded plant material.
Hemicellulolytic enzymes, i.e. hemicellulases, include xylanase, .beta.-xylosidase and esterases, which actively cleave hemicellulosic material through hydrolysis. Among these xylanase and esterase enzymes cleave the xylan and acetyl side chains of birch xylan and the remaining xylo-oligomers are unsubstituted and can thus be hydrolysed with .beta.-xylosidase only. In addition, several less known side activities have been found in enzyme preparations which hydrolyse hemicellulose. Hemicellulolytic enzymes are produced by the fermentation of certain microorganisms, such as fungi of the Aspergillus or Trichoderma genera. The culture medium as such or enzyme fractions separated from it can be used as an enzyme preparation in the hydrolysis of hemicellulose.
Under hydrolytic reaction conditions hemicellulolytic enzymes free in a solution retain their activity only for a relatively short period of time. They are expensive to use and difficult to recover. Enzymes immobilized on a solid carrier are more stable than free enzymes, and they are also more easily reusable, wherefore several processes have been developed for immobilizing hemicellulolytic enzymes.
One major problem in the hydrolysis of a technical hemicellulose solution by immobilized enzyme is the high salt content of the solution. An ionic material shows a tendency to displace the enzyme from the surface of the carrier so that the column loses rapidly its enzyme activity.
Hemicellulolytic enzymes have been immobilized, for example, on silica gel, alumina, or steel (Oguntimeim, G. B., Proc. Annu. Biochem, Eng. Symp. 1978, vol. 8, p. 27-37), on porous glass (Rogalski, J. et al., Enzyme Microb. Technol. 7 (1985) No. 8, p. 27-37), on fibres (Tavobilov, I. et al.; Chemical Abstracts 104 (1986) 30924n) or on benzoquinone silochrome carrier (Balcere D. et al.; Chemical Abstracts 100 (1984) 99098f). The use of silica gel carrier has also been suggested by Shimizu (Biotechnology and Bioengineering, 29 (1987) p. 36-241) and Allenza et al. (Biotechnology and Bioengineering Symp. No. 17 (1986) John Wiley & Sons 1987). Puls J. et al. (Trans. Tech. Sect., Can. Pulp Pap. Assoc. 3 p. 64-72 and U.S. Pat. No. 4,275,159) have used porous glass beads, silica gel beads and sea sand as carrier in the immobilization of hemicellulase and xylanase fractions.
In all these prior art immobilization techniques, the enzyme is fixed onto the carrier using an additive which activates the surface of the carrier and/or forms a covalent bond between the carrier and the enzyme. In the process described in the above-mentioned U.S. Pat. No. 4,275,159 (Puls et al.) an enzyme fraction containing mainly xylanase and an enzyme fraction containing mainly .beta.-xylosidase are immobilized separately on different carriers using in both cases glutaraldehyde, carbodiimide or TiCl.sub.4 as a fixing additive, and the resulting two enzyme preparations are used in the hydrolysis of xylan.
Oguntimein et al. (Biotechnol. Bioeng. 22 (1980) p. 1127-1142) have studied the immobilization of .beta.-xylosidase purified from a commercial enzyme preparation produced by Aspergillus niger on ten different carriers. It was found that the immobilization was very difficult to perform and satisfactory results with regard to activity and stability were obtained only with an enzyme fixed with TiCl.sub.4 on alumina and with an enzyme fixed with glutaraldehyde on porous alkyl amine silica gel.
Weckstrom, L. and Leisola, M. (Advances in Biotechnology. Edit. M. Moo-Young and C. W
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Heikkila Heikki
Mustranta Annikka
Poutanen Kaisa
Sarkki Marja-Leena
Marx Irene
Xyrofin Oy
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