Over-expression of DAAO and catalase in Kluyveromyces marxianus through media optimization, permeabilization and GA stabilization techniques.

Abstract:

:The selected thermotolerant, lactose-utilizing yeast strain Kluyveromyces marxianus NBIMCC 8362 possesses high specific d-amino acid oxidase activity (60Ug(-1)), which was increased nine-fold (545Ug(-1)) by design of the growth medium and conditions for d-amino oxidase induction. Applying an optimized simple and rapid procedure for chemical permeabilization of K. marxianus cells with the cationic detergent cetyltrimethylammonium bromide, the enzyme activities (d-amino acid oxidase and catalase) of the cells have been further increased for up to 43- and 58-fold, respectively. However, the enzyme activities of the permeabilized cells decreased rapidly due to the leakage of the enzymes. Treating the permeabilized cells with 0.1% glutaraldehyde at 4°C for 10min stabilized the enzyme in the cells and prevented their outflow. The process is stable for 10 cycles and the productivity measured was 16.6mmmoll(-1)h(-1). The d-alanine transformation efficiency of K. marxianus permeabilized and GA entrapted cells was 98%.

journal_name

Enzyme Microb Technol

authors

Kostova DD,Petrova VY,Kujumdzieva AV

doi

10.1016/j.enzmictec.2007.08.010

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

113-20

issue

2

eissn

0141-0229

issn

1879-0909

pii

S0141-0229(07)00278-5

journal_volume

42

pub_type

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