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Increasing the scale of peroxidase production by S treptomyces sp. strain BSII #1
Author(s) -
Musengi A.,
Khan N.,
Le RoesHill M.,
Pletschke B.I.,
Burton S.G.
Publication year - 2014
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/jam.12380
Subject(s) - peroxidase , aeration , streptomyces , bioreactor , food science , strain (injury) , lignin peroxidase , chemistry , inducer , enzyme , biochemistry , microbiology and biotechnology , biology , bacteria , organic chemistry , anatomy , gene , genetics
Aims To optimize peroxidase production by S treptomyces sp. strain BSII #1, up to 3 l culture volumes. Methods and Results Peroxidase production by S treptomyces sp. strain BSII #1 was optimized in terms of production temperature and p H and the use of lignin‐based model chemical inducers. The highest peroxidase activity (1·30 ± 0·04 U ml −1 ) in 10 ml culture volume was achieved in a complex production medium (p H 8·0) at 37°C in the presence of 0·1 mmol l −1 veratryl alcohol, which was greater than those reported previously. Scale‐up to 100 and 400 ml culture volumes resulted in decreased peroxidase production (0·53 ± 0·10 and 0·26 ± 0·08 U ml −1 , respectively). However, increased aeration improved peroxidase production with the highest production achieved using an airlift bioreactor (4·76 ± 0·46 U ml −1 in 3 l culture volume). Conclusions Veratryl alcohol (0·1 mmol l −1 ) is an effective inducer of peroxidase production by S treptomyces sp. strain BSII #1. However, improved aeration increased peroxidase production in larger volumes without the use of an inducer, surpassing induced yields in an optimized small‐scale process. Significance and Impact of the Study Only a limited number of reports in literature have focused on the up‐scaling of bacterial peroxidase production. There remains opportunity for feasible large‐scale production of bacterial peroxidases with potentially novel biocatalytic properties.