دانلود رایگان مقاله انگلیسی تعامل بین لاکتوفرین و پروتئین های آب پنیر و تأثیر آن بر ژل شدن پروتئین های آب پنیر - الزویر 2018

عنوان فارسی
تعامل بین لاکتوفرین و پروتئین های آب پنیر و تأثیر آن بر ژل شدن پروتئین های آب پنیر
عنوان انگلیسی
Interaction between lactoferrin and whey proteins and its influence on the heat-induced gelation of whey proteins
صفحات مقاله فارسی
0
صفحات مقاله انگلیسی
7
سال انتشار
2018
نشریه
الزویر - Elsevier
فرمت مقاله انگلیسی
PDF
کد محصول
E8282
رشته های مرتبط با این مقاله
صنایع غذایی
گرایش های مرتبط با این مقاله
علوم مواد غذایی
مجله
شیمی مواد غذایی - Food Chemistry
دانشگاه
College of Light Industry and Food Engineering - Guangxi University - Nanning - China
کلمات کلیدی
لاکتوفرین، پروتئین آب پنیر، ژلاتین، مدول الاستیک، پتانسیل زتا، توزیع اندازه
چکیده

ABSTRACT


In this paper, the influence of lactoferrin (LF) on the structural development of whey protein isolate (WPI) gels during heating was investigated. The results demonstrated that the presence of sufficient LF could improve the strength and elasticity of WPI gels. When 30% LF was added, the elastic modulus of WPI gels increased from 254 ± 31 and 413 ± 58 Pa to 3222 ± 105 and 2730 ± 131 Pa at pH 6.7 and 5.8, respectively. The addition of LF improved the water holding capacity (WHC) of WPI gels at pH 6.7, while no improvement was observed at pH 5.8. LF interacted with whey proteins differently at pH 6.7 and 5.8 during heating. The LF/whey proteins complexes formed at pH 6.7 had smaller sizes and narrower size distributions than those formed at pH 5.8.

نتیجه گیری

4. Conclusion


The aforementioned results clearly demonstrated that the incorporation of LF into WPI gel can change its structural properties, with these changes depending on pH and structural properties of LF. The denatured LF molecules could crosslink whey proteins through disulphide bonds and hydrophobic interactions. WPI gel obtained at pH 5.8 had higher elastic modulus and water holding capacity than that at pH 6.7. The addition of LF increased the gel strength at both pH values. However, stronger and more uniform gels were obtained at pH 6.7 compared to pH 5.8 in the presence of high concentrations of LF (20% and 30%). The findings from this research are of both practical and theoretical significance for the utilization of LF in gelled protein products.


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