Please use this identifier to cite or link to this item:
|Title:||Protease treatment for the stabilization of rice bran: Effects on lipase activity, antioxidants, and lipid stability|
|Publisher:||American Association of Cereal Chemists|
|Abstract:||© 2014 AACC International, Inc. Rice bran lipid is rapidly made rancid by endogenous lipase enzymes. To inactivate rice bran lipase, an enzymatic hydrolytic method was developed and then compared with the thermal method. The efficiency of five proteolytic enzymes including trypsin, chymotrypsin, papain, bromelain, and Flavourzyme enzyme to stabilize rice bran was investigated. Moreover, the antioxidant content and storage stability of enzymatically stabilized rice bran (ESRB), thermally stabilized rice bran (TSRB), and raw rice bran (RRB) were studied. Trypsin, chymotrypsin, and papain showed a higher rate of hydrolysis than bromelain and Flavourzyme enzyme. After 120 min of hydrolysis, rice bran hydrolyzed by trypsin, chymotrypsin, and papain inactivated 80, 86, and 79% of lipase activity, respectively, whereas lipase activity of rice bran hydrolyzed by bromelain and Flavourzyme enzyme was higher than the initial rice bran. With a similar lipase inactivation level, the cheaper papain was used to produce ESRB. Total phenolics content of ESRB was 52.89 and 94.10% higher than in RRB and TSRB, respectively. In addition, γ-oryzanol content in ESRB was 2.23- and 2.05-fold of that in RRB and TSRB, respectively. Lipase activity of RRB increased throughout the two months of storage, whereas no change in lipase activity was observed in ESRB and TSRB. At the end of storage, free fatty acid contents of RRB, TSRB, and ESRB were 15.30, 4.67, and 3.92%, respectively. We propose enzymatic hydrolysis by papain for stabilization of rice bran with high antioxidant content and storage stability.|
|Appears in Collections:||AGRO: Journal Articles|
Files in This Item:
There are no files associated with this item.
Items in CMUIR are protected by copyright, with all rights reserved, unless otherwise indicated.