Research and Development Center for Industrial Fermentations

Research and Development Center for Industrial Fermentations

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Cavello I.A.,Research and Development Center for Industrial Fermentations | Cavalitto S.F.,Research and Development Center for Industrial Fermentations | Hours R.A.,Research and Development Center for Industrial Fermentations
Applied Biochemistry and Biotechnology | Year: 2012

Paecilomyces lilacinus (LPS 876) efficiently degraded keratin in chicken feather during submerged cultivation producing extracellular proteases. Characterization of crude protease activity was done including its compatibility in commercial detergents. Optimum pH and temperature were 10.0 and 60 °C, respectively. Protease activity was enhanced by Ca2+ but was strongly inhibited by PMSF and by Hg2+ suggesting the presence of thioldependent serine proteases. The crude protease showed extreme stability toward non-ionic (Tween 20, Tween 85, and Triton X-100) and anionic (SDS) surfactants, and relative stability toward oxidizing agent (H2O2 and sodium perborate). In addition, it showed excellent stability and compatibility with various solid and liquid commercial detergents from 30 to 50 °C. The enzyme preparation retained more than 95% of its initial activity with solid detergents (Ariel™ and Drive™) and 97% of its original activity with a liquid detergent (Ace™) after pre-incubation at 40 °C. The protective effect of polyols (propylene glycol, PEG 4000, and glycerol) on the heat inactivation was also examined and the best results were obtained with glycerol from 50 to 60 °C. Considering its promising properties, P. lilacinus enzymatic preparation may be considered as a candidate for use in biotechnological processes (i.e., as detergent additive) and in the processing of keratinous wastes. © Springer Science+Business Media, LLC 2012.


Butiuk A.P.,Research and Development Center for Industrial Fermentations | Adachi O.,Yamaguchi University | Hours R.A.,Research and Development Center for Industrial Fermentations
Biocatalysis and Agricultural Biotechnology | Year: 2015

The potential of yerba mate (. Ilex paraguariensis) to induce chlorogenate hydrolase (EC 3.1.1.42, CHase) activity in different fungal strains has been investigated. CHase was highly induced in mycelia of Aspergillus niger AKU 3302 grown in Czapek medium containing yerba mate extract as inducer. Different materials derived from yerba mate processing were examined as CHase activity inducers. All yerba mate samples produced CHase activity and a concentrated aqueous yerba mate extract was selected as the most convenient inducer. A response surface methodology was used to assess the simultaneous effect of inducer concentration and induction duration on enzyme production. The experimental design revealed that the optimum CHase production was achieved after long induction times (≥25. h) and low inducer concentrations (0.1-0.2% w/v, dry basis). © 2015 Elsevier Ltd.


Cavello I.A.,Research and Development Center for Industrial Fermentations | Chesini M.,Research and Development Center for Industrial Fermentations | Hours R.A.,Research and Development Center for Industrial Fermentations | Cavalitto S.F.,Research and Development Center for Industrial Fermentations
Journal of Microbiology and Biotechnology | Year: 2013

Six nonpathogenic fungal strains isolated from alkaline soils of Buenos Aires Province, Argentina (Acremonium murorum, Aspergillus sidowii, Cladosporium cladosporoides, Neurospora tetrasperma, Purpureocillium lilacinum (formerly Paecilomyces lilacinus), and Westerdikella dispersa) were tested for their ability to produce keratinolytic enzymes. Strains were grown on feather meal agar as well as in solid-state and submerged cultures, using a basal mineral medium and "hair waste" as sole sources of carbon and nitrogen. All the tested fungi grew on feather meal agar, but only three of them were capable of hydrolyzing keratin, producing clear zones. Among these strains, P. lilacinum produced the highest proteolytic and keratinolytic activities, both in solid-state and submerged fermentations. The medium composition and culture conditions for the keratinases production by P. lilacinum were optimized. Addition of glucose (5 g/l) and yeast extract (2.23 g/l) to the basal hair medium increased keratinases production. The optimum temperature and initial pH for the enzyme production were 28°C and 6.0, respectively. A beneficial effect was observed when the original concentration of four metal ions, present in the basal mineral medium, was reduced up to 1:10. The maximum yield of the enzyme was 15.96 U c /ml in the optimal hair medium; this value was about 6.5-fold higher than the yield in the basal hair medium. These results suggest that keratinases from P. lilacinum can be useful for biotechnological purposes such as biodegradation (or bioconversion) of hair waste, leading to a reduction of the environmental pollution caused by leather technology with the concomitant production of proteolytic enzymes and protein hydrolyzates. © 2013 by The Korean Society for Microbiology and Biotechnology.


Castaneda M.T.,Research and Development Center for Industrial Fermentations | Adachi O.,Yamaguchi University | Hours R.A.,Research and Development Center for Industrial Fermentations
Journal of Industrial Microbiology and Biotechnology | Year: 2015

l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remove l-phenylalanine (l-Phe) from different commercial protein hydrolysates. A casein acid hydrolysate (CAH, l-Phe ~2.28 %) was employed as a model substrate. t-Cinnamic acid resulting from deamination of l-Phe was extracted, analyzed at λ = 290 nm, and used for PAL activity determination. Optimum reaction conditions, optimized using successive Doehlert design, were 35 mg mL−1 of CAH and 800 mU mL−1 of PAL, while temperature and pH were 42 °C and 8.7, respectively. Reaction kinetics of PAL with CAH was determined under optimized conditions. Then, removal of l-Phe from CAH was tested. Results showed that more than 92 % of initial l-Phe was eliminated. Similar results were obtained with other protein hydrolysates. These findings demonstrate that PAL is a useful biocatalyst for l-Phe removal from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for PKU patients. © 2015, Society for Industrial Microbiology and Biotechnology.

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