Abstract：
:Cross-linked enzyme aggregates (CLEAs) are reported for the first time for a recombinant acetyl xylan esterase (AXE) from Bacillus pumilus. With this enzyme, CLEAs production was most effective using 3.2M (80%-saturation) ammonium sulfate, followed by cross-linking for 3h with 1% (v/v) glutaraldehyde. Particle size was a key determinant of the CLEAs activity. The usual method for generating particles, by short-time vortexing was highly inefficient in terms of enzyme activity yields. In contrast, the use of long-time vortexing increased activity recovery, and a novel approach consisting in the utilization of a commercial mechanical cell disruptor which is based on a reciprocating movement recovered all the enzyme activity in few seconds. In the CLEAs thus produced, the enzyme was much more resistant to shear, heat and extreme pH values than the soluble enzyme. The CLEAs were highly effective in transforming fully 7-amino cephalosporanic acid and cephalosporin C into their corresponding desacetyl derivatives, which are important advanced intermediates in the production of semisynthetic beta-lactam antibiotics. The operational stability of such CLEAs was remarkable, with a half life of 45 cycles. Therefore, the new methodology used here should decrease the industrial cost of the CLEAs, both in terms of biocatalyst production and reusability.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Montoro-García S,Gil-Ortiz F,Navarro-Fernández J,Rubio V,García-Carmona F,Sánchez-Ferrer Adoi
10.1016/j.biortech.2009.08.016subject
Has Abstractpub_date
2010-01-01 00:00:00pages
331-6issue
1eissn
0960-8524issn
1873-2976pii
S0960-8524(09)01046-3journal_volume
101pub_type
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