4.7 Article

Thermal behavior, microstructure and protein quality of squid fillets dried by far-infrared assisted heat pump drying

Journal

FOOD CONTROL
Volume 36, Issue 1, Pages 102-110

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodcont.2013.08.006

Keywords

Heat pump drying; Far-infrared radiation; Thermal characteristics; Microstructure; Electrophoresis; Protein quality; Squid

Funding

  1. Shanghai Natural Science Foundation [11ZR1416100]
  2. National Natural Science Foundation of China [31271955]
  3. National Science & Technology Pillar Program [2013BAD 18B02]
  4. International Advanced Agricultural Science and Technology Introduction Program (948 Program) [2013-S18]
  5. National High Technology Research and Development Program of China (863 Program) [2012AA092303]
  6. Wilmar Award Program for Outstanding Young Teachers

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The effects of far-infrared assisted heat pump drying on the thermal behavior, microstructure and protein quality of squid fillets were studied. Heat pump drying (HPD) alone or in combination with far-infrared radiation (FIR) at the power of 100, 500 and 800 W, 40 degrees C and 2 m s(-1) air velocity were compared. Nitrogen fractions, proteases activities, amino acid profile, microstructure, SDS-PAGE and protein quality of fresh and dried squid samples were examined. Results showed that glutamic acid, aspartic acid, lysine and isoleucine are the dominant amino acids in all samples. The total contents of essential amino acid and non-essential amino acid, essential amino acid index, estimated protein efficiency ratio and biological value were not significantly different among all squid samples (P > 0.05). The cathepsins B and L activity decreased along with increased power supplied to the FIR heater. Drying increased the denaturation enthalpy (Delta H) of myosin and actin as well as the thermal transition temperature (T-max) of actin compared with the fresh, non-dried squid. HPD-treated samples had the highest T-max of myosin and HPD + 1FIR-treated samples had the lowest T-max of actin. Electrophoretic profiles showed the disappearance of 24, 57, 93, 105, 121 and 172 kDa bands, while the new concomitant bands were appeared at 30, 37, 102 and 154 kDa. Dried squid muscle had dense and firm microstructure, and high FIR intensity resulted in more compact and coherent structure of dried squid. Generally, HPD in combination with FIR did not induce significant loss of amino acid quality in the dried squid fillets. (C) 2013 Elsevier Ltd. All rights reserved.

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