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1.
Braz. arch. biol. technol ; 60: e16160541, 2017. tab, graf
Artigo em Inglês | LILACS | ID: biblio-951463

RESUMO

ABSTRACT Rock phosphate (RP) is traditionally solubilized by chemical process causing high cost and environmental pollution. To reduce process cost and protect environment, RP solubilization by Aspergillus japonicus was studied and its mechanisms were discussed. Results show that A. japonicus could effectively solubilize RP in NBRIP medium. RP solubilization by A. japonicus included direct and indirect actions of the strain on RP. Cells of A. japonicus attached rapidly to RP surface and the RP surface was seriously corroded by the strain. A. japonicus excreted multiple organic acids, and followed by a significant increase of titratable acidity and decrease of pH in the culture. A positive correlation between content of soluble phosphate and quantity of titratable acidity but a negative correlation between content of soluble phosphate and pH were observed. Results of abiotic solubilization of RP using organic and inorganic acids indicated that the release of soluble phosphate was significantly lower than that of inoculated with A. japonicus. Higher release of soluble phosphate and pH reduction achieved when using ammonium nitrogen rather than nitrate nitrogen.

2.
Braz. arch. biol. technol ; 55(5): 671-676, Sept.-Oct. 2012. ilus
Artigo em Inglês | LILACS | ID: lil-651649

RESUMO

Enzymes obtained by fermentation processes offer a number of advantages and have been widely researched and used throughout the world. This study aimed to partially characterise an inulinase produced from palm and cassava peel. The enzyme was produced via the solid-state fermentation of Aspergillus japonicus URM5633. The optimal temperatures were 50ºC and 55ºC, and the optimal pH values were 5.2 and 3.4 for inulinase fermentatively produced from palm and cassava peel, respectively. The thermostability measurements for inulinase produced in palm showed that the relative activity remained below 100% until 30 minutes of stability for all temperatures, but reached 106.8% at a temperature of 50ºC after 60 minutes. Inulinase from the crude extract of cassava peel was pH stable and only decreased to 55% of the maximal activity over the course of the assay, suggesting that this enzyme can be used in inulinase production and can be utilized in food industries.

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