کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
222791 464296 2016 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Changes of protein secondary structures of pollock surimi gels under high-temperature (100 °C and 120 °C) treatment
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی مهندسی شیمی (عمومی)
پیش نمایش صفحه اول مقاله
Changes of protein secondary structures of pollock surimi gels under high-temperature (100 °C and 120 °C) treatment
چکیده انگلیسی


• The changes of the protein secondary structures of the surimi gels were studied.
• The secondary structure of the surimi gels treated with 100–120 °C was mainly random coil.
• The random coil structure damaged as treating temperature increased.
• High-temperature treatment resulted in serious damage to the network structure of the surimi gels.

To produce instant surimi products, sterilization is essential. Previous studies found that the gel strength of surimi decreased significantly with treating temperature increasing from 100 °C to 120 °C, which affected the texture of the products. In this study, the changes of the secondary structures of surimi gels were studied to provide new train of thought for the improvement of the texture of high temperature treated surimi gels. Surimi gels from Alaska Pollock were obtained by heating and maintaining their central temperature at 100 °C and 120 °C for 10 min under a constant pressure (0.12 MPa). Infrared (IR) spectroscopy and Raman spectroscopy showed that the secondary structure of the surimi gels with high temperature (≥100 °C) treatment was mainly random coil and the random coil structure damaged with treating temperature increasing, which made the frames of the network structure become much more fragile and the holes become larger, leading to the destruction of the textural properties of the surimi gels.

The secondary structure of the pollock surimi gels with high-temperature (≥100 °C) treatment was mainly random coil. With treating temperature increasing, the random coil structure damaged, resulting in the disappearance of myosin heavy chain and significant decrease of actin content. In addition, the protein molecules aggregated. So the frames of the network structure became much more fragile and the holes became larger, leading to the destruction of the textural properties of the surimi gels.Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Food Engineering - Volume 171, February 2016, Pages 159–163
نویسندگان
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