تغییرات فیزیکوشیمیایی ایزوله پروتئین آب پنیر پس از واسرشته شدن، آبکافت آنزیمی و درهم تنیدن

نوع مقاله: مقاله پژوهشی

نویسندگان

1 استادیار-گروه علوم و مهندسی صنایع غذایی - دانشکده کشاورزی - دانشگاه کردستان- سنندج - ایران

2 استاد- گروه علوم و مهندسی صنایع غذایی- دانشکده مهندسی و فناوری کشاورزی- پردیس کشاورزی و منابع طبیعی- دانشگاه تهران- کرج- ایران

چکیده

در مطالعه اخیر، خصوصیات فیزیکوشیمیایی ایزوله پروتئین آب پنیر و ترکیبات حاصله از آن شامل پروتئین آب پنیر واسرشت، پروتئین آب پنیر درهم تنیده، آبکافت پروتئین آب پنیر و آبکافت پروتئین آب پنیر درهم تنیده مورد بررسی قرار گرفت. آبکافت آنزیمی و فرآیند در هم تنیدن به ترتیب توسط آنزیم پپسین (30 دقیقه در دمای 37 درجه­ سلسیوس) و آنزیم ترانس­گلوتامیناز (20 ساعت در دمای 50 درجه سلسیوس) انجام پذیرفت. نتایج بدست آمده نشان داد پروتئین آب پنیر واسرشته شده توسط حرارت متوسط اندازه کمتر (44 نانومتر) و پتانسیل زتا (19‒) بیشتری نسبت به پروتئین بکر داشته است. ایجاد اتصالات عرضی توسط ترانس گلوتامیناز نیز شدت جمعیت مولکول­های با متوسط اندازه بیشتر را در هر دو نمونه پروتئین واسرشت و آبکافت شده کاهش داده است. همچنین قدرت پاداکسیدانی آبکافت پروتئین آب پنیر در طی در هم­تنیدن و افزایش طول زنجیره پپتیدی از 398/0 به 519/0 افزایش پیدا کرده بود. نتایج طیف سنجی فروسرخ تبدیل فوریه نشان داد که درهم تنیدن آنزیمی به دلیل تشکیل باندهای جدید C‒N بین کربن آلفا لیزین و گروه آمین نوع اول گلوتامین، محل پیک مربوطه را در هر دو نمونه پروتئین آب پنیر درهم­تنیده و آبکافت پروتئینی درهم­تنیده جابه­جا کرده است.

کلیدواژه‌ها

موضوعات


عنوان مقاله [English]

Changes of Physico-Chemical Properties of Whey Protein after Denaturation, Enzymatic Hydrolysis and Cross-Linking

نویسندگان [English]

  • Himan Nourbakhsh 1
  • Zahra Emam jomeh 2
1 Assistant Professor, Department of Food Science and Engineering , Faculty of Agriculture, University of Kurdistan, Sanandaj, Iran
2 Professor, Department of Food Science and Engineering, Faculty of Agricultural engineering and Technology, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran
چکیده [English]

In the current research, physico-chemical properties of whey protein isolate (WPI) and its resulting compounds including denatured whey protein isolate (DWPI), cross-linked whey protein isolate (CWPI), whey protein hydrolysate (WPH) and cross-linked whey protein hydrolysate (CWPH) were analyzed. Enzymatic hydrolysis and cross-linking were performed by pepsin (at 37°C for 30 min) and transglutaminase (at 50°C for 20 h), respectively. The obtained results stated that, by moderate heat, DWPI had smaller average size (44 nm) and more zeta-potential rather than native WPI. Intensity of the number of molecules with higher average particle size has been reduced by cross-linking of both DWPI and WPH using transglutaminase. Also, the antioxidant activity of WPH was increased from 0.398 to 0.519 through cross-linking and making larger peptide chain. The result of fourier-transform infrared spectroscopy (FTIR) indicated the enzymatic cross-linking owing to the formation of new C−N bonds between the α-carbon of lysine and the primary amine group of glutamine displaced the corresponding band at both CWPI and CWPH samples.

کلیدواژه‌ها [English]

  • Antioxidant activity
  • Particle size
  • pepsin
  • transglutaminase

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