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Immobilization of D‐ribulose‐1,5‐bisphosphate carboxylase/oxygenase: A step toward carbon dioxide fixation bioprocess
Author(s) -
Chakrabarti Subhra,
Bhattacharya Sumana,
Bhattacharya Sanjoy K.
Publication year - 2003
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10515
Subject(s) - rubisco , oxygenase , chemistry , ribulose 1,5 bisphosphate , carbon dioxide , immobilized enzyme , pyruvate carboxylase , carbon fixation , agarose , ribulose , chromatography , biochemistry , enzyme , organic chemistry
Immobilization of D‐ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) from spinach leaves is described. This enzyme enables the fixation of carbon dioxide on a five‐carbon sugar D‐ribulose‐1,5‐bisphosphate (RuBP). Two different immobilization methods were employed: dicyclohexylcarbodiimide coupling on nylon membrane matrix and dimethylpimelimidate immobilization on protein A agarose. The reusability of immobilized enzymes, coupling efficiency, and temperature–activity relationship of soluble and immobilized Rubisco are presented. The immobilization imparted greater thermal and storage stability. The thermal deactivation rates of the immobilized enzymes were considerably lower than those of the soluble enzyme. © 2003 Wiley Periodicals. Biotechnol Bioeng 81: 705–711, 2003.