L-asparaginase from Aspergillus oryzae spp.: effects of production process and biochemical parameters
Autor: | Santa Maria Del Rosário Orrillo Lindo, Marília Crivelari da Cunha, Jessika Gonçalves dos Santos Aguilar, Hélia Harumi Sato, Ruann Janser Soares de Castro |
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Rok vydání: | 2021 |
Předmět: |
0106 biological sciences
Aspergillus Plackett–Burman design biology 010405 organic chemistry General Medicine biology.organism_classification 01 natural sciences Biochemistry 0104 chemical sciences chemistry.chemical_compound Hydrolysis chemistry Aspergillus oryzae 010608 biotechnology Acrylamide Casein Fermentation Food science Lactose Biotechnology |
Zdroj: | Preparative Biochemistry & Biotechnology. 52:253-263 |
ISSN: | 1532-2297 1082-6068 |
Popis: | L-asparaginases prevent the formation of acrylamide, a substance commonly found in foods subjected to heat and that also contains reducing sugars and L-asparagine. This work aimed to select a strain of Aspergillus spp. able to produce L-asparaginase and to optimize the fermentation parameters, the partial purification and biochemical characterization were also performed. The Aspergillus oryzae IOC 3999 was selected due to its greater enzymatic activity: 1443.57 U/mL of L-asparaginase after 48 h of fermentation. The optimized conditions allowed for an increase of 223% on the L-asparaginase production: 2.9% lactose, 2.9% L-asparagine and 0.7% hydrolyzed casein, 0.152% KH2PO4, 0.052% KCl and MgSO4, 0.001% of CuNO3.3H2O, ZnSO4.7H2O and FeSO4.7H2O adjusted to pH 7.0; added a concentration of 5.05x106 spores/mL at 30 °C for 100 rpm. A purification factor of 2.11 was found and the molecular mass was estimated at 20.8 kDa. The enzyme showed optimum activity at 60 °C and pH 5 and stability at 50 °C for 1 h. The enzyme presented desirable biochemical characteristics, mainly the acid pH stability, indicating that the enzyme would work well in food matrices due to the closeness of pH, meaning that it could be a potential option for use in the food industry. |
Databáze: | OpenAIRE |
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