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Efficient Immobilization of Lecitase in Gelatin Hydrogel and Degumming of Rice Bran Oil Using a Spinning Basket Reactor
Author(s) -
Sheelu Gurrala,
Kavitha G.,
Fadnavis Nitin W.
Publication year - 2008
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-008-1261-7
Subject(s) - chemistry , gelatin , bran , immobilized enzyme , enzyme assay , glutaraldehyde , chromatography , enzyme , bioreactor , food science , biochemistry , organic chemistry , raw material
Immobilization of Lecitase (Phospholipase A1) in gelatin hydrogel and its stability is studied with a view to utilizing the immobilized enzyme for degumming rice bran oil. Excellent retention of enzyme activity (>80%) is observed in hydrogel containing 43.5% gelatin crosslinked with glutaraldehyde. Compared to the free enzyme which has a broad pH‐activity profile (6.5–8.0), the activity of the immobilized enzyme is strongly dependent on pH and has a pH‐optimum of pH 7.5. The optimum temperature of enzyme activity increases from 37 to 50 °C. Compared to the free enzyme which loses all its activity in 72 h at 50 °C, the immobilized enzyme retains its activity in full. The immobilized enzyme has been used efficiently in a spinning basket bioreactor for the degumming of rice bran oil with 6 recycles without loss of enzyme activity. The phosphorus content of the oil decreases from 400 ppm to 50–70 ppm in each cycle. After charcoal treatment and dewaxing, a second enzymatic treatment brings down the phosphorus content to <5 ppm.