Optimizing the immobilization of lipase enzyme (Aspergillus oryzae) in the silica and silica-cellulose matrix by adsorption method

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

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Pemurnian dan Karakterisasi Enzim Lipase dari Aspergillus oryzae pada Kopra Berjamur

Jurnal Natur Indonesia ◽

10.31258/jnat.14.1.26-31 ◽

2012 ◽

Vol 14 (1) ◽

pp. 26

Author(s):

Seniwati Dali Dali ◽

Abdul Rauf Patong ◽

Muhammad Noor Jalaluddin ◽

Pirman Andi Parenrengi

Keyword(s):

Ammonium Sulphate ◽

Aspergillus Oryzae ◽

Enzyme Purification ◽

Maximum Activity ◽

Crude Enzyme ◽

Lipase Catalysis ◽

Lipase Enzyme ◽

Km Value ◽

Ammonium Sulphate Fractionation

An investigation on purification and characterization of lipase enzyme production Aspergillus oryzae from copra by fermentation of oliveoil has been carried out. This enzyme can be produced by fermenting olive oil in a medium containing Aspergillus oryzae. Crude enzyme isobtained by centrifuging the medium cultures containing Aspergillus oryzae at 3500 rpm for 30 minutes and than adding 0.2 M borat buffer(pH 8.2). Enzyme activity was determined from paranitrophenol as product of lipase catalysis of paranitrophenylbutirat (0.2 M) assubstrate measured by the Vorderwulbecke method. Prepurification process was by ammonium sulphate fractionation. Precipitation60-80% ammonium sulphate produced maximum activity of enzyme. Purification by Q sepharosa FF and sephadex G-75 collumchromatography produced four and three fractions with purifity of 12.85 and 20.25 times than crude enzyme respectively. Characterizationof this enzyme showed optimum condition at pH 8.2, temperature at 350C, the Km value at 0.046 M, and Vmaks is 1.926 μmol/menit and themolecular weight at 40.7 kDa.

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Koji mold (Aspergillus oryzae)

AccessScience ◽

10.1036/1097-8542.900130 ◽

2015 ◽

Keyword(s):

Aspergillus Oryzae ◽

Koji Mold

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Expression of an α-galactosidase from Saccharomyces cerevisiae in Aspergillus awamori and Aspergillus oryzae

Journal of Industrial Microbiology & Biotechnology ◽

10.1038/sj.jim.7000217 ◽

2002 ◽

Vol 28 (2) ◽

pp. 97-102 ◽

Cited By ~ 1

Author(s):

R-A Murphy ◽

R-F-G Power

Keyword(s):

Saccharomyces Cerevisiae ◽

Aspergillus Oryzae ◽

Aspergillus Awamori

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The Effects of Brinolase (Fibrinolytic Enzyme from Aspergillus Oryzae) on Platelet Aggregation of Dog and Man

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649039 ◽

1972 ◽

Vol 28 (01) ◽

pp. 031-048 ◽

Cited By ~ 4

Author(s):

W. H. E Roschlau ◽

R Gage

Keyword(s):

Platelet Aggregation ◽

Aspergillus Oryzae ◽

Degradation Products ◽

Blood Platelet ◽

Human Platelets ◽

Fibrinolytic Enzyme ◽

Inhibitory Effects ◽

Blood Platelet Aggregation

SummaryInhibition of blood platelet aggregation by brinolase (fibrinolytic enzyme from Aspergillus oryzae) has been demonstrated with human platelets in vitro and with dog platelets in vivo and in vitro, using both ADP and collagen as aggregating stimuli. It is suggested that the optimal inhibitory effects of brinolase occur indirectly through the generation of plasma fibrinogen degradation products, without compromising platelet viability, rather than by direct proteolysis of platelet structures.

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