Journal
PROCESS BIOCHEMISTRY
Volume 73, Issue -, Pages 109-116Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2018.07.013
Keywords
Chemical immobilization of immobilized enzymes; Enzyme amination; Enzyme crosslinking; Enzyme modulation; Enzyme stabilization; Hydrolysis of proteins
Categories
Funding
- MINECO from Spanish Government [CTQ2017-86170-R]
- Algerian Ministry of higher education and scientific research
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Ficin extract immobilized on glyoxyl-agarose was chemically modified using carbodiimide and ethylenediamine (full or partial amination of the carboxylic groups of the enzyme) or glutaraldehyde (modifying primary amino groups) under different conditions. Aminated enzyme altered its activity versus casein and benzoyl-arginine-p-nitroanilide (BANA), e.g., the activity versus casein even slightly increased while versus BANA it decreased, being this more significant at pH 9 (the fully aminated biocatalyst increased the activity versus casein by 10% but it decreased more than 5 folds versus BANA), greatly altering the enzyme specificity. The amination improved the enzyme stability at pH 5 while stability was impoverished at pH 9. Glutaraldehyde treatment usually decreased the activity versus BANA while it improved the activity versus casein (by around a factor of 2 when using 1% glutaraldehyde). Enzyme thermostability was enhanced, mainly at pH 7. This permitted to have more linear casein hydrolysis courses at pH 7 and 66 degrees C compared to the unmodified enzyme. Amination followed by glutaraldehyde treatment drove to the almost full enzyme inactivation. Thus, these treatments may be considered interesting for preparing an improved biocatalyst of ficin, mainly in proteolytic applications, and may be considered (mainly the amination) a possibility to further improve enzyme immobilization.
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