Continuous and Batch Production of Chloroperoxidase by Mycelial Pellets of Caldariomyces fumago in an Airlift Fermentor.
نویسندگان
چکیده
Batch and continuous production of the extracellular heme glycoprotein chloroperoxidase (CPO) was studied with an airlift fermentor. We induced Caldariomyces fumago CMI 89362 to form pellets by transferring a small inoculum volume in preculture prior to growth in a 1-liter fermentor. Continuous replacement of the fructose-salts medium (dilution rate, 0.008 h) supported continuous CPO formation at an average concentration of 128 +/- 10 mg of CPO liter for 8 days. Optimum CPO production rates averaged 1.2 +/- 0.1 mg of CPO h at dilution rates below 0.033 h. Varying the carbohydrate content of the feed solution or the time of starting the feed did not significantly alter the amount of CPO produced. Batch fermentation in the airlift fermentor resulted in maximum CPO concentrations of 280 +/- 80 mg of CPO liter, although on two separate occasions CPO concentrations reached 400 to 450 mg liter, which was double the amount obtained by free hyphae in shake flask culture.
منابع مشابه
Semicontinuous and Continuous Production of Chloroperoxidase by Caldariomyces fumago Immobilized in k-Carrageenan.
Three strains of Caldariomyces fumago were immobilized in 4% k-carrageenan and tested for semicontinuous production of chloroperoxidase (CPO). Over an 80-day period, growing in defined medium, C. fumago strains CMI 89362 and ATCC 11925 produced enzyme concentrations of 99 and 71 mg/liter, respectively, during six production periods of 12 to 14 days, while C. fumago DAOM 137632 produced only 24 ...
متن کاملDraft Genome Sequence of the Chloroperoxidase-Producing Fungus Caldariomyces fumago Woronichin DSM1256
We report here the draft genome sequence of the chloroperoxidase (EC 1.11.1.10)-producing ascomycete Caldariomyces fumago Its genome was assembled into 511 contigs with a total size of 25 Mb. The G+C content is 51.4%, and 9,806 putative protein-coding genes were predicted. Eight heme-thiolate peroxidase genes, including two chloroperoxidase genes, were found.
متن کاملC-terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?
The Caldariomyces fumago chloroperoxidase (CPO) is synthesised as a 372-aa precursor which undergoes two proteolytic processing events: removal of a 21-aa N-terminal signal peptide and of a 52-aa C-terminal propeptide. The Aspergillus niger expression system developed for CPO was used to get insight into the function of this C-terminal propeptide. A. niger transformants expressing a CPO protein...
متن کاملBiocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors.
The encapsulation of chloroperoxidase from Caldariomyces fumago (CPO) in block copolymer polymersomes is reported. Fluorescence and electron microscopy show that when the encapsulating conditions favour self-assembly of the block copolymer, the enzyme is incorporated with concentrations that are 50 times higher than the enzyme concentration before encapsulation. The oxidation of two substrates ...
متن کاملExpression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme.
The Caldariomyces fumago chloroperoxidase was successfully expressed in Aspergillus niger. The recombinant enzyme was produced in the culture medium as an active protein and could be purified by a three-step purification procedure. The catalytic behavior of recombinant chloroperoxidase (rCPO) was studied and compared with that of native CPO. The specific chlorination activity (47 units/nmol) of...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 55 1 شماره
صفحات -
تاریخ انتشار 1989