Effects of thermal processing on digestion stability and immunoreactivity of the Litopenaeus vannamei matrix.

Many types of shellfish, including shrimp, are sometimes cooked before ingestion. Hence, it is necessary to investigate how cooking (boiling, pressure treatment or none (raw)) affects the structure, digestibility and immunoreactivity of multi-component shrimp muscle. Protein extraction, simulated gastrointestinal digestion, immunoreactivity, immunoglobulin E (IgE)-mediated human mast cell degranulation, morphology, particle size and UV absorbance scanning were used to investigate changes in the shrimp muscle upon treatment.

Effect of blend ratio and pH on the physical properties of edible composite films prepared from silver carp surimi and skin gelatin.

The effect of blend ratio and pH on the physical properties of surimi-gelatin composite films was investigated. Tensile strength (TS), film water solubility and soluble proteins of composite films increased with the increasing proportion of gelatin, while elongation at break (EAB) decreased. The TS of neutral films with the same ratio of surimi and gelatin were lowest, while increased at acidic or alkaline conditions.

Purification and characterization of pepsinogens and pepsins from the stomach of rice field eel (Monopterus albus Zuiew).

Three pepsinogens (PG1, PG2, and PG3) were highly purified from the stomach of freshwater fish rice field eel (Monopterus albus Zuiew) by ammonium sulfate fractionation and chromatographies on DEAE-Sephacel, Sephacryl S-200 HR. The molecular masses of the three purified PGs were all estimated as 36 kDa using SDS-PAGE. Two-dimensional gel electrophoresis (2D-PAGE) showed that pI values of the three PGs were 5.

Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin).

Crustacean allergy is a significant health problem around the world, and tropomyosin (TM) represents the major allergen of crustaceans. The aim of this study was to evaluate three processing methods (boiling, CUB, HPS) and identify the one method that is most effective in the degradation of TM and reduction of its IgE-binding reactivity, and make it easier to be decomposed during gastrointestinal digestion. SDS-PAGE analysis indicated that boiling had little impact on the digestive stability of TM.

Comparative study of in vitro digestibility of major allergen, tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei).

Background: Stability in simulated gastric fluid is supposed to be an important parameter for the estimation of food allergenicity. In the present study, the digestive stability of allergenic protein tropomyosin (TM) and other food proteins from Grass prawn and Pacific white shrimp in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion assay system was investigated and comparatively studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blotting, and inhibition enzyme-linked immunosorbent assay (ELISA).

Results: In the SGF system, proteins such as actin and myosin heavy chain (MHC) were rapidly degraded within a short period of time, while TM was relatively resistant to pepsin digestion.

Comparative study of in vitro digestibility of major allergen tropomyosin and other food proteins of Chinese mitten crab (Eriocheir sinensis).

Background: China is the largest producer and consumer of aquatic products in the world; however, many people in China suffer from allergies upon consuming crab. Stability in simulated gastric fluid is regarded as an important parameter for the estimation of food allergenicity.

Results: The digestive stability of allergenic protein tropomyosin (TM) and other food proteins from Chinese mitten crab in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion assay systems was investigated and compared by SDS-PAGE, western blot and inhibition ELISA.

Purification and characterization of a gelatinolytic metalloproteinase from the skeletal muscle of red sea bream (Pagrus major).

A gelatinolytic metalloproteinase (gMP) from red sea bream ( Pagrus major ) skeletal muscle was highly purified by ammonium sulfate fractionation and column chromatographies including (diethylamino)ethyl (DEAE)-Sephacel, phenyl-Sepharose, and gelatin-Sepharose. Purified gMP revealed two bands with molecular masses of 52 and 55 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. The 55 kDa band is quite possibly a glycosylated form of the 52 kDa band.

Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) by in vitro gastrointestinal digestion.

Stability in simulated gastric fluid is regarded as an important parameter for the estimation of food allergenicity. In this study, the digestive stability of allergenic protein tropomyosin (TM) and other food proteins from mud crab in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion assay system was investigated and compared by SDS-PAGE and Western blot. In SGF system, proteins such as actin and the original band of myosin heavy chain (MHC) were rapidly degraded within a short period of time, while TM was relatively resistant to pepsin digestion.

Study on pepsinogens and pepsins from snakehead (Channa argus).

Three pepsinogens (PG1, PG2, and PG3) were highly purified from the stomach of freshwater fish snakehead (Channa argus) by ammonium sulfate fractionation, anion exchange, and gel filtration. Two-dimensional gel electrophoresis and native-PAGE analysis revealed that their molecular masses were 37, 38, and 36 kDa and their isoelectric points 4.8, 4.