Mohd Asraf Mohd Zainudin
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Preferred name
Mohd Asraf Mohd Zainudin
Official Name
Mohd Asraf, Mohd Zainudin
Alternative Name
Mohd Zainudin, Mohd Asraf
Zainudin, M. A.M.
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Scopus Author ID
55539687700
Researcher ID
AAV-4476-2020

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  • Publication
    Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol
    ( 2021-01-01)
    Mohd Asraf Mohd Zainudin
    ;
    Jongberg S.
    ;
    Lund M.N.
    Plant polyphenols applied as natural antioxidant ingredients, are known to bind to cysteine residues on meat proteins. The aim of this study was to examine the effect of light exposure on the formation of cysteine-phenol adduct in meat added 4-methylcatechol (4MC), a model polyphenol, during storage through quantitative LC-MS/MS-based analysis. Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased significantly (by 50%) when stored under light in oxygen at 4 °C for 7 days as compared to storage in the dark. This was reflected by a significant decrease in thiol concentrations in the same sample. Gel electrophoresis showed loss in myosin heavy chain (MHC), and a resulting increase in cross-linked MHC (CL-MHC) and larger protein polymers in samples added 4MC. Protein blots stained with nitroblue tetrazolium (NBT) showed intensive protein-polyphenol binding in the meat samples added 4MC, but no major differences between storage conditions.
      23  1
  • Publication
    Quantitation of Protein Cysteine-Phenol Adducts in Minced Beef Containing 4-Methyl Catechol
    ( 2020-02-26)
    Arsad S.S.
    ;
    Mohd Asraf Mohd Zainudin
    ;
    De Gobba C.
    ;
    Jongberg S.
    ;
    Larsen F.H.
    ;
    Lametsch R.
    ;
    Andersen M.L.
    ;
    Lund M.N.
    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.
      1  24