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  1. Sarker ZI, Elgadir MA, Ferdosh S, Akanda JH, Manap MY, Noda T
    Molecules, 2012;17(5):5733-44.
    PMID: 22628045 DOI: 10.3390/molecules17055733
    The objective of this study was to investigate the effect of selected biopolymers on the rheological properties of surimi. In our paper, we highlight the functional properties and rheological aspects of some starch mixtures used in surimi. However, the influence of some other ingredients, such as cryoprotectants, mannans, and hydroxylpropylmethylcellulose (HPMC), on the rheological properties of surimi is also described. The outcome reveals that storage modulus increased with the addition of higher levels of starch. Moreover, the increasing starch level increased the breaking force, deformation, and gel strength of surimi as a result of the absorption of water by starch granules in the mixture to make the surimi more rigid. On the other hand, the addition of cryoprotectants, mannans, and HPMC improved the rheological properties of surimi. The data obtained in this paper could be beneficial particularly to the scientists who deal with food processing field.
    Matched MeSH terms: Muscle Proteins/chemistry*
  2. Zhang Q, Noryati I, Cheng LH
    J Food Sci, 2008 Mar;73(2):E82-7.
    PMID: 18298729 DOI: 10.1111/j.1750-3841.2007.00627.x
    Chicken breast muscle powder (CBMP) and modified waxy cornstarch (MWCS) blends were prepared at different pH conditions (pH 4, 5, 6, 7, 8, and 9). The blends were characterized by light microscopy, frequency sweep, flow analysis, and freeze-thaw stability analysis. Light microscopy showed that the blend structure was coarse at pH conditions close to the isoelectric point of protein and became finer with increasing pH. Frequency sweep demonstrated that the blend was more liquid-like with relatively lower storage (G') and loss (G'') moduli as the pH was increased from pH 4 to pH 9. Flow analysis revealed that thixotropy behavior was evident in samples treated at pHs 4 and 5, whereas antithixotropy was shown by those adjusted to pHs 6, 7, 8, and 9. The CBMP-MWCS blends were found to show better freeze-thaw stability at pH 8 that could be attributed to the formation of a highly interactive network structure of CBMP and MWCS.
    Matched MeSH terms: Muscle Proteins/chemistry*
  3. Arsad SS, Zainudin MAM, De Gobba C, Jongberg S, Larsen FH, Lametsch R, et al.
    J Agric Food Chem, 2020 Feb 26;68(8):2506-2515.
    PMID: 32013414 DOI: 10.1021/acs.jafc.9b07752
    Thiol groups of cysteine (Cys) residues in proteins react with quinones, oxidation products of polyphenols, to form protein-polyphenol adducts. The aim of the present work was to quantify the amount of adduct formed between Cys residues and 4-methylcatechol (4MC) in minced beef. A Cys-4MC adduct standard was electrochemically synthesized and characterized by liquid chromatography-mass spectrometry (LC-MS) as well as NMR spectroscopy. Cys-4MC adducts were quantified after acidic hydrolysis of myofibrillar protein isolates (MPIs) and LC-MS/MS analysis of meat containing either 500 or 1500 ppm 4MC and stored at 4 °C for 7 days under a nitrogen or oxygen atmosphere. The concentrations of Cys-4MC were found to be 2.2 ± 0.3 nmol/mg MPI and 8.1 ± 0.9 nmol/mg MPI in meat containing 500 and 1500 ppm 4MC, respectively, and stored for 7 days under oxygen. The formation of the Cys-4MC adduct resulted in protein thiol loss, and ca. 62% of the thiol loss was estimated to account for the formation of the Cys-4MC adduct for meat containing 1500 ppm 4MC. Furthermore, protein polymerization increased in samples containing 4MC as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the polymerization was found to originate from protein-polyphenol interactions as evaluated by a blotting assay with staining by nitroblue tetrazolium.
    Matched MeSH terms: Muscle Proteins/chemistry
  4. Nurkhoeriyati T, Huda N, Ahmad R
    J Food Sci, 2012 Jan;77(1):S91-8.
    PMID: 22260136 DOI: 10.1111/j.1750-3841.2011.02519.x
    The physicochemical properties and sensory analysis of duck meatballs containing duck meat surimi-like material during frozen storage were evaluated. Properties of meatballs containing duck surimi-like material prepared by acid solubilization (ACDS), alkaline solubilization (ALDS), and conventional processing (CDS) as well as duck mince (as the control, CON) were compared. ACDS had significantly higher (P < 0.05) moisture and protein content and lower fat content compared with CON. The thiobarbituric acid-reactive substances (TBARS) value of all samples increased as the storage time increased up to week 8 (P < 0.05), but thereafter it decreased in most of the samples. ACDS and ALDS had significantly higher TBARS values (P < 0.05), and these values remained higher than those of the other samples throughout the frozen storage period. Addition of surimi-like material to the meatballs had significant effects (P < 0.05) on springiness, gumminess, and chewiness values of all samples. Ingredients and frozen storage affected most sensory attributes in samples significantly (P<0.05). No significant increase in growth of organisms occurred during 12-wk frozen storage The results indicate that acid-alkaline solubilization methods improve both physicochemical and sensory properties of duck meatballs containing duck surimi-like material. Thus, these techniques should be applicable to product development of duck surimi-like material.
    Matched MeSH terms: Muscle Proteins/chemistry*
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