Use of carbohydrase to enhance protein extraction efficiency and antioxidative properties of oat bran protein hydrolysates

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• 作者：Sara Jodayree^a ; ^b ; Jeffrey C. Smith^b ; Apollinaire Tsopmo^a ; ^b ; ^{apollinaire_tsopmo@carleton.ca}
• 关键词：Oat bran ; Carbohydrase ; Antioxidant ; Peptide ; Mass spectrometry
• 刊名：Food Research International
• 出版年：2012
• 出版时间：April, 2012
• 年：2012
• 卷：46
• 期：1
• 页码：69-75
• 全文大小：508 K

文摘

In this study, medium oat bran samples were treated with four cell wall carbohydrases degrading enzymes (viscozyme? L, ¦Á-amylase, amyloglucosidase, celluclast?). Their effects on protein extraction efficiency and, on antioxidant properties of obtained protein isolates and resulting alcalase hydrolysates were investigated. The results showed that sample pre-treated with amyloglucosidase (8 units/g) had the higher protein content (82 % ) while celluclast (5-60 endo-glucanase units (EGU)/g) pre-treated samples had protein content similar to that of control (54 % ). In the oxygen radical absorbance assay (ORAC) all samples of protein isolates had significantly higher peroxyl radical scavenging activity than the control. The sample pre-treated with alpha-amylase (2300 units/g) displayed the highest activity with an ORAC value of 165 ¡À 16 ¦ÌM Trolox Equivalents (TE)/g. Proteins were hydrolyzed with alcalase and radical scavenging activities of hydrolysates assessed by ORAC and HO?radical assays. Sample pre-treated with viscozyme 1.5 Fungal Beta-glucanase Units (FBU)/g was the more active in both assays: ORAC value 521 ¡À 53 ¦ÌM TE/g and HO?radical inhibition 26.3 ¡À 1.5 % . A tandem mass spectrometric analysis of multiple charged ions within the hydrolysates allowed the identification of four new peptides.