رسالة جامعية
Functional and structural characteristics of acid-hydrolyzed whey protein concentrate
| العنوان: | Functional and structural characteristics of acid-hydrolyzed whey protein concentrate |
|---|---|
| المؤلفون: | Alizadeh Pasdar, Nooshin |
| مرشدي الرسالة: | Alli, I. (advisor) |
| بيانات النشر: | McGill University, 1995. |
| سنة النشر: | 1995 |
| المجموعة: | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| مصطلحات موضوعية: | Whey products., Globular proteins., Protein hydrolysates. |
| جغرافية الموضوع: | Master of Science (Department of Food Science and Agricultural Chemistry.) |
| الوصف: | Whey Protein Concentrate (WPC) is used as a functional ingredient in many food products. To increase the applicability of WPC as well as other food proteins, it is often necessary to enhance the functional properties of the protein. Various protein modification techniques can be used for this purpose; this includes chemical, physical and enzymatic modification. In present study acid hydrolysis, a chemical modification, was investigated as a means to improve functionality of WPC, emulsifying, foaming and gelatin. Most of the previous work on WPC has been directed at enzymatic hydrolysis. Dispersions of WPC (8%) in organic acids (0.5 N, 1 N and 1.5 N acetic acid, citric acid phosphoric acid and mixture of these acids) were subjected to acid hydrolysis (6, 18 and 48 h) and the effects of this modification on functional properties was assessed. The degrees of hydrolysis were measured and freeze-dried hydrolysates were evaluated for their foam capacity and stability, emulsifying activity and stability index and toughness. Highest foam capacity was found in the hydrolysate obtained using 0.5 N acetic acid (6 h hydrolysis, foaming capacity of 140%); acid hydrolysis increased foam stability, in general. In addition, acid hydrolysis did not affect emulsifying activity index but gave higher emulsifying stability index and toughness of prepared gels. Results of PAGE indicated that acidic modification led to progressive decrease in the $ alpha$-lactalbumin and BSA. $ alpha$-lactalbumin was found to be the most sensitive protein with significant degradation after 6 h hydrolysis. (Abstract shortened by UMI.) |
| Original Identifier: | oai:collectionscanada.gc.ca:QMM.22844 |
| نوع الوثيقة: | Electronic Thesis or Dissertation |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | alephsysno: 001481800; proquestno: MM07993; Theses scanned by UMI/ProQuest. |
| الإتاحة: | http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=22844Test |
| حقوق: | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| رقم الانضمام: | edsndl.LACETR.oai.collectionscanada.gc.ca.QMM.22844 |
| قاعدة البيانات: | Networked Digital Library of Theses & Dissertations |
| الوصف غير متاح. |