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差示扫描量热法分析热和压力对与各种类型增塑剂混合的大豆粉中蛋白质变性的影响

Differential Scanning Calorimetry Analysis of the Effects of Heat and Pressure on Protein Denaturation in Soy Flour Mixed with Various Types of Plasticizers.

作者信息

Kweon Meera, Slade Louise, Levine Harry

机构信息

Dept. of Food Science and Nutrition, Pusan National Univ., Busan, 46241, South Korea.

Food Polymer Science Consultancy, Morris Plains, N.J., 07950, U.S.A.

出版信息

J Food Sci. 2017 Feb;82(2):314-323. doi: 10.1111/1750-3841.13616. Epub 2017 Jan 10.

Abstract

The effects of heat and pressure on protein denaturation in soy flour were explored by an experimental design that used pressure (atmospheric to 600 MPa), temperature (room to 90 °C), time (1 to 60 min), and type of aqueous plasticizer (NaCl, sucrose, betaine, and lactobionic acid (LBA)) as factors. When 50% (w/w) soy flour-water paste was high hydrostatic pressure (HHP)-treated for 20 min at 25 °C, the treatment at 200 MPa showed a small effect on denaturation of only the 7S soy globulin, but the treatment at 600 MPa showed a significant effect on denaturation of both the 7S and 11S soy globulins. The treatment at 60 °C showed a less-pronounced effect on denaturation of the 11S globulin, even at 600 MPa, but that at 90 °C showed a similar extent of denaturation of the 11S globulin at 600 MPa to that at 25 °C. Chaotropic 2N NaCl, 50% sucrose-, 50% betaine-, or 50% LBA-water solutions showed protective effects on protein denaturation during HHP treatment at 25 °C. Although LBA enhanced the extent of thermostability of soy protein less than did 2N NaCl, LBA exhibited better stabilization against pressure. The results from DSC analysis demonstrated that thermostable soy proteins were not always barostable.

摘要

通过一项实验设计探究了加热和压力对大豆粉中蛋白质变性的影响,该实验设计将压力(常压至600兆帕)、温度(室温至90℃)、时间(1至60分钟)以及水性增塑剂类型(氯化钠、蔗糖、甜菜碱和乳糖酸(LBA))作为因素。当50%(w/w)的大豆粉 - 水糊在25℃下进行20分钟的高静水压(HHP)处理时,200兆帕的处理对仅7S大豆球蛋白的变性影响较小,但600兆帕的处理对7S和11S大豆球蛋白的变性均有显著影响。60℃的处理对11S球蛋白的变性影响较小,即使在600兆帕时也是如此,但90℃的处理在600兆帕时11S球蛋白的变性程度与25℃时相似。离液剂2N氯化钠、50%蔗糖、50%甜菜碱或50% LBA - 水溶液在25℃的HHP处理过程中对蛋白质变性具有保护作用。尽管LBA增强大豆蛋白热稳定性的程度不如2N氯化钠,但LBA在抗压力方面表现出更好的稳定性。差示扫描量热法(DSC)分析结果表明,热稳定的大豆蛋白并不总是耐压稳定的。

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