scholarly journals BREWERY-RESIDUE UTILIZATION OF A FRESHLY ISOLATED A. NIGER SP. UPT-03 FOR PROTEASE PRODUCTION UNDER SOLID-STATE FERMENTATION

Engevista ◽  
2012 ◽  
Vol 15 (1) ◽  
pp. 61 ◽  
Author(s):  
Salah Din Mahmud Hasan ◽  
Citieli Giongo ◽  
Sonia Aparecida Reis Lopes-Shikida ◽  
Sérgio Luiz de Lucena ◽  
Mônica Lady Fiorese

The operation parameters used in solid-state fermentation (SSF) support the growth of filamentous fungi, which grow on solid substrates producing important metabolites such as proteases. The aim of this work is to obtain fungal proteases by SSF using the residues of a local brewery industry (barley bagasse and trub), that have high contents of proteins and soluble matter such as carbohydrates, vitamins, and mineral salts. The methodology includes the preparation of the residues, the screening of microorganisms, evaluation of the operation conditions for SSF using factorial design, purification and partial characterization of the protease. The results indicate that A. niger sp. UPT-03 isolated from the residue shows higher yields in terms of enzyme production (0.36 U gdm-1 h-1). The purification with DEAE-cellulose resulted in protease recovery with 30-fold of purification with a specific activity of 550 U mg protein-1. Higher proteolytic activity of purified enzyme was obtained at pH 5.5 and 55 ºC.

2012 ◽  
Vol 47 (1) ◽  
pp. 99-104 ◽  
Author(s):  
G Dharani ◽  
NS Kumaran

The purpose of this work is to study the optimized cultural conditions for the production of amylase by Aspergillus niger in solid state and submerged liquid fermentation. Four solid substrates banana peel, corn, potato and tapioca with different moisture conditions were taken for solid state fermentation (SSF). Basal medium was used for submerged liquid fermentation (SLF) with different pH (3 to 8), temperature (25, 30, 35 and 40ºC), carbon concentration (1, 2 and 3 g) and nitrogen source (0.1, 0.2 and 0.3 g). In SSF, tapioca yielded highest amylase activity and specific activity (4.43U/ml and 4.58U/mg) at 50% moisture content. In SLF, 2 g starch and 0.3 g peptone concentration showed 0.78 and 1.23 U/ml amylase activities under the optimum pH (5) and temperature (30ºC) the amylase activities reached to 0.86 U/ml and 0.76 U/ml respectively. In SSF using tapioca as substrate the enzyme yield is about five times higher than that achieved with submerged liquid culture. DOI: http://dx.doi.org/10.3329/bjsir.v47i1.7310 Bangladesh J. Sci. Ind. Res. 47(1), 99-104, 2012


2021 ◽  
Vol 93 (suppl 3) ◽  
Author(s):  
FELYPE T.B. ROCHA ◽  
ROMERO M.P. BRANDÃO-COSTA ◽  
ANNA GABRIELLY D. NEVES ◽  
KETHYLEN B.B. CARDOSO ◽  
THIAGO P. NASCIMENTO ◽  
...  

2021 ◽  
Author(s):  
Roheena Abdullah ◽  
◽  
Maham Asim ◽  
Muhammad Nadeem ◽  
Kinza Nisar ◽  
...  

Proteases have gained more commercial value to date due to multiple applications in different industrial sectors. Current research was aimed to use the cheaper agricultural waste for optimal protease production. Maximum level of protease production was achieved at 37 °C, incubation period of 24 h, pH 9.0, inoculum size 3%, 1.5 g sucrose as a carbon source and 30% moisture content by using solid-state fermentation. Among the various inorganic and organic nitrogen sources, ammonium nitrate and yeast extract tremendously increased the production of protease. Among metal ions and surfactants tested, Ca2+ and Tween 40 showed the optimal protease production. The purification of protease was carried out by ammonium salt precipitation followed by sephadex G-100 gel filtration chromatography. The purification resulted in 1.3 fold of purified protease with a specific activity of 51.5 and a total yield of 37.5 %. Molecular weight of purified protease was predicted upon SDS-PAGE with a single band of ~36 kDa. The protease was quite stable over a temperature range of 35-45 °C and pH 7-9 with maximal activity at 40 °C and pH 9. The kinetic parameters Vmax (maximum rate) and Km (Michaelis-Menten constant) were calculated as 0.307 U/g and 11.2 mg/mL, respectively. The alkaline protease significantly de-hair the goat skin and successfully removed the animal blood stain from cotton cloth.


2008 ◽  
Vol 83 (7) ◽  
pp. 1012-1018 ◽  
Author(s):  
Jarun Chutmanop ◽  
Sinsupha Chuichulcherm ◽  
Yusuf Chisti ◽  
Penjit Srinophakun

BioResources ◽  
2014 ◽  
Vol 9 (4) ◽  
Author(s):  
Valesca Weingartner Montibeller ◽  
Luciana Porto de Souza Vandenberghe ◽  
Antonella Amore ◽  
Carlos Ricardo Soccol ◽  
Leila Birolo ◽  
...  

2016 ◽  
Vol 15 (28) ◽  
pp. 1511-1519 ◽  
Author(s):  
Becker Onofre Sideney ◽  
Abatti Dirceu ◽  
Refosco Douglas ◽  
Antonio Tessaro Amarildo ◽  
Alisson Becker Onofre Jean ◽  
...  

2013 ◽  
Vol 27 (3) ◽  
pp. 3776-3781 ◽  
Author(s):  
Lydia Toscano ◽  
Gisela Montero ◽  
Lourdes Cervantes ◽  
Margarita Stoytcheva ◽  
Velizar Gochev ◽  
...  

2018 ◽  
Vol 81 (1) ◽  
Author(s):  
Halifah Pagarra ◽  
Roshanida A. Rahman ◽  
Nur Izyan Wan Azelee ◽  
Rosli Md Illias

Polygalacturonases represent an important member of pectinases group of enzymes with immense industrial applications. The activity of exo-polygalacturonase produced by Aspergillus niger was studied in solid state fermentation (SSF) using Nephrolepis biserrata leaves as substrate. Central composite design (CCD) was used to optimize four significant variables resulted from the screening process that has been initially analyzed for the production of exo-polygalacturonase which are incubation time, temperature, concentration of pectin and moisture content. The optimum exo-polygalacturonase production obtained was 54.64 U/g at 120 hours of incubation time, temperature at 340C, 5.0 g/L of pectin concentration and 75.26% of moisture content. For partial characterization of exo-polygalacturonase, the optimum temperature and pH were obtained at 50°C and pH 4.0, respectively. SDS-PAGE analysis showed that molecular weight of exo-polygalacturonase were 35 and 71 kDa. This study has revealed a significant production of exo-polygalacturonase by A. niger under SSF using cheap and easily available substrate and thus could found immense potential application in industrial sectors and biotechnology


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