NDLI: Physicochemical properties and biological activities of ovine caseinate hydrolysates

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Erratum to: NMR spectroscopy as a screening tool to validate nutrition labeling of milk, lactose-free milk, and milk substitutes based on soy and grains

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Physicochemical properties and biological activities of ovine caseinate hydrolysates

Content Provider	Springer Nature Link
Author	Daroit, Daniel J. Corrêa, Ana Paula F. Canales, Manuel Mancilla Coelho, Julise G. Hidalgo, María E. Tichota, Deise M. Risso, Patricia H. Brandelli, Adriano
Copyright Year	2012
Abstract	Caseins are the precursors of bioactive peptides, which can be released through enzymatic hydrolysis and subsequently be incorporated into food products. This investigation evaluated the antioxidant and antimicrobial activities, as well as the physicochemical features, of ovine sodium caseinate (NaCAS) subjected to proteolysis. A Bacillus sp. P45 protease preparation was utilized in the hydrolysis of ovine NaCAS, for up to 7 h. Absorbance and intrinsic fluorescence spectra suggested that the hydrolysis of NaCAS exposed aromatic amino acids to the aqueous media. Following a slight decrease in the surface hydrophobicity (S $_{0}$) observed up to 2 h of hydrolysis, S $_{0}$ increased in the hydrolysates from 3 to 7 h, indicating exposure of hydrophobic groups on the surface of the generated peptides. An increase in the antioxidant properties, evaluated by the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid method, was observed following hydrolysis up to 4 h. One-hour hydrolysates inhibited the growth of Salmonella enteritidis, Escherichia coli, Corynebacterium fimi, and Listeria monocytogenes, showing antifungal activity of the hydrolysates. The gelation ability of the hydrolysates was maintained, as evaluated through acid aggregation induced by glucono-δ-lactone (GDL). Although aggregation occurred at slower rates than that of nonhydrolyzed samples, the compactness of the aggregates formed from 1- to 2-h hydrolysates was comparable to that of nonhydrolyzed NaCAS. The final state of aggregates formed from NaCAS/hydrolysate mixtures (4:1) was not altered. Thus, these functional hydrolysates might be potentially added to dairy products manufactured through acid-induced aggregation, without significantly affecting this process.摘要: 酪蛋白是生物活性肽的前体物质,生物活性肽可以通过酶水解酪蛋白释放出来继而成为食用级的产品。本文考察并评价了绵羊酪蛋白酸钠经蛋白酶水解后水解物的抗氧化和抑菌活性及其物化特性。芽孢杆菌属(Bacillus sp.)p45 蛋白酶被用来水解绵羊酪蛋白酸钠,水解时间为7h。吸光度和内源荧光光谱表明酪蛋白酸钠被水解后,一些芳香族氨基酸暴露于水相介质。当水解时间为2h,水解物表面疏水性缓慢下降,当水解时间为3-7h, 水解物疏水性有所增加,该结果表明,疏水性基团暴露在新产生的肽的表面。水解物抗氧化特性通过2 ,2-联氮-二(3-乙基-苯并噻唑-6-磺酸)二铵盐(ABTS)法来评价,水解时间为4h时, 其抗氧化特性增加。水解时间为1h时,水解物能够抑制肠炎沙门杆菌、大肠杆菌、棒状杆菌属和单核细胞增生利斯特菌的生长,证明了水解物有抗真菌的能力。酪蛋白酸钠水解物的凝胶能力通过葡萄糖酸内酯酸聚合诱导来评价。虽然水解物凝聚发生的速率低于没有水解的酪蛋白酸钠,但是,水解时间为1和2h水解物的致密性与没有水解的酪蛋白酸钠是相似的。酪蛋白酸钠与水解物以4:1混合形成的凝聚物的最终状态保持不变。因此,这些功能性的水解物可以通过酸诱导凝聚,可潜在的添加到乳制品加工中,对乳制品的加工过程不会产生影响。
Starting Page	335
Ending Page	351
Page Count	17
File Format	PDF
ISSN	19585586
Journal	Dairy Science & Technology
Volume Number	92
Issue Number	4
e-ISSN	19585594
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-06-08
Publisher Place	Paris
Access Restriction	Subscribed
Subject Keyword	Ovine caseinate Protein hydrolysates Gelation Acid aggregation Bioactive peptides Food Science Microbiology Agriculture
Content Type	Text
Resource Type	Article
Subject	Biochemistry Food Science

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