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酶改性马铃薯蛋白分离物的功能和构象特性。

Functional and conformational properties of proteolytic enzyme-modified potato protein isolate.

机构信息

Department of Food Science and Technology, Sari Agricultural Sciences and Natural Resources University, Sari, Iran.

Department of Basic Sciences, Sari Agricultural Sciences and Natural Resources University, Sari, Iran.

出版信息

J Sci Food Agric. 2020 Feb;100(3):1320-1327. doi: 10.1002/jsfa.10148. Epub 2019 Dec 11.

DOI:10.1002/jsfa.10148
PMID:31742702
Abstract

BACKGROUND

Potato protein hydrolysates (PPHs) were preparedwith Alcalase on intact potato protein isolates (PPI), with differenthydrolysis times (0.5-4 h), and functional and conformational properties of resultant hydrolysates were investigated.

RESULTS

The degree of hydrolysis changed during incubation. Peptide bond cleavage increased and hydrolysis progressed rapidly. Gel electrophoresis showed that, by increasing the hydrolysis time, peptides with an apparent molecular weight below 20 kDa increased. It also revealed that, among potato protein components, patatin was more sensitive to Alcalase® hydrolysis than protease inhibitors. Enzymatic hydrolysis significantly enhanced the solubility and foam capacity of PPHs, but impaired foam stability (P < 0.05). Limited enzymatic hydrolysates (0.5PPH) at the interface improved the emulsion activity and stability index. These emulsions also had the smallest z-average and polydispersity index and showed the highest zeta potential. Fourier-transform infrared spectrometry (FTIR) analysis indicated extensive disruption of hydrogen bonds in PPHs, besides augmentation of α-helices and β-turns, and a decline in the β-sheets in the secondary structure of the PPHs was shown.

CONCLUSION

Potato protein isolate, especially 0.5PPH, has good functional and conformational properties. Overall, our results provide new insights into the use of potato protein hydrolysates as a functional food component in the food industry. © 2019 Society of Chemical Industry.

摘要

背景

使用 Alcalase 在完整的马铃薯蛋白分离物(PPI)上制备马铃薯蛋白水解物(PPH),水解时间不同(0.5-4 小时),并研究了所得水解产物的功能和构象特性。

结果

水解过程中水解度发生变化。肽键的裂解增加,水解迅速进行。凝胶电泳表明,随着水解时间的增加,分子量低于 20 kDa 的肽增加。结果还表明,在马铃薯蛋白成分中,相对于蛋白酶抑制剂,类脂酶更容易受到 Alcalase®水解的影响。酶解显著提高了 PPH 的溶解度和泡沫能力,但降低了泡沫稳定性(P<0.05)。有限的酶解产物(0.5PPH)在界面处提高了乳液的活性和稳定性指数。这些乳液的 z 均粒径和多分散指数最小,表明其表面的zeta 电位最高。傅里叶变换红外光谱(FTIR)分析表明,PPH 中的氢键广泛断裂,同时α-螺旋和β-转角增加,二级结构中的β-折叠减少。

结论

马铃薯蛋白分离物,特别是 0.5PPH,具有良好的功能和构象特性。总的来说,我们的结果为将马铃薯蛋白水解物作为功能性食品成分在食品工业中的应用提供了新的见解。 © 2019 化学工业协会。

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