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Immobilization of glucose isomerase to cellulose
Author(s) -
Sirotti David A.,
Emery Alden
Publication year - 1978
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.690240615
Subject(s) - glucose 6 phosphate isomerase , reagent , cellulose , catalysis , chemistry , cyanogen bromide , bromide , fructose , active site , covalent bond , hydrolysis , chromatography , organic chemistry , enzyme , biochemistry , peptide sequence , gene
Abstract Glucose isomerase was covalently bonded to Solka‐floc and DEAE cellulose by several techniques. The best results were obtained with techniques that opened the crystalline structure of the cellulose and kept it that way during immobilization. The most active catalyst was prepared by mercerizing Solka‐floc, cross‐linking it in that expanded configuration with epoxides, and immobilizing the enzyme with cyanogen bromide. The second most active catalyst was made using DEAE cellulose and a mixture of di and tri‐epoxides as immobilization reagent. The practical consequences of the results were tested by designing reactors to produce high fructose syrup using the activity and stability of several of the preparations. Since the activity decays with time, equations were developed to give the optimum time of running before the catalyst was discarded. The most promising one was the second most active; the most active catalyst yielded a production cost three times as great because of the large quantities of cyanogen bromide needed.

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