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Klaus Biemann – One of the best experts on this subject based on the ideXlab platform.

  • amino acid sequence of a protease inhibitor isolated from sarcophaga bullata determined by mass spectrometry
    Protein Science, 2008
    Co-Authors: Ioannis A Papayannopoulos, Klaus Biemann

    Abstract:

    The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.

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  • Amino acid sequence of a protease inhibitor isolated from Sarcophaga bullata determined w
    , 1992
    Co-Authors: Klaus Biemann

    Abstract:

    The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.

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Cunliu Zhou – One of the best experts on this subject based on the ideXlab platform.

  • l arginine and l lysine degrade troponin t and l arginine dissociates actomyosin their roles in improving the tenderness of chicken breast
    Food Chemistry, 2020
    Co-Authors: Yinyin Zhang, Hongmei Fang, Daojing Zhang, Yajun Huang, Li Chen, Pengqi Bao, Cunliu Zhou

    Abstract:

    Abstract This work investigated the effects of L-arginine (Arg) and L-lysine (Lys) on the tenderness of chicken breast and explored the possible mechanisms underlying this effect for the first time. The results showed that both Arg and Lys decreased the shear force and increased the pH value, sarcomere length and myofibrillar fragmentation index as well as degraded the troponin-T by keeping calpain activity in chicken breast. In addition, Arg effectively reduced Ca2+/Mg2+-ATPase activities and promoted actomyosin dissociation. These results indicated that both Arg and Lys could enhance the tenderness of chicken breast, and it could also explain why Arg was more effective than Lys in improving the tenderness of chicken breast. These results will help facilitate the development of industrial-scale methods for improving the tenderness of meat products.

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  • effects of basic amino acid on the tenderness water binding capacity and texture of cooked marinated chicken breast
    Lwt – Food Science and Technology, 2020
    Co-Authors: Yinyin Zhang, Hongmei Fang, Daojing Zhang, Yajun Huang, Li Chen, Pengqi Bao, Cunliu Zhou

    Abstract:

    Abstract This work investigated the effects of basic amino acids such as l -arginine (Arg)/ l -lysine (Lys) on the physicochemical properties of cooked marinated chicken breast (CMCB) as well as the possible mechanism underlying these effects. The results indicated that shearing force decreased from 13.3 N to 10.0 N and cooking loss decreased from 38.3 g/100 g–26 g/100 g when Lys increased from 0 g/100 g–0.4 g/100 g, while shearing force decreased to 8.8 N and cooking loss decreased to 28 g/100 g at 0.4 g Arg/100 g. Furthermore, Arg/Lys improved the textural parameters and increased pH value. Low field-nuclear magnetic resonance showed that Arg shortened the relaxation times of T21 from 50 ms to 38 ms and Arg/Lys increased the peak area percentage (P21) for T21 from 93.6 to 97. Arg/Lys promoted the extraction of salt-soluble meat proteins from 54 mg/g to 78.6 mg/g. Scanning electron microscopy illustrated that Arg and Lys narrowed the gaps between muscle fibers at 0.6 g/100 g and at 0.4 g/100 g, respectively. The results disclosed that Arg/Lys could improve the physicochemical properties of CMCB, and thus showing a potential for the manufacture of cooked marinated meat products.

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  • l-Lysine/l-arginine/l-cysteine synergistically improves the color of cured sausage with NaNO2 by hindering myoglobin oxidation and promoting nitrosylmyoglobin formation.
    Food Chemistry, 2019
    Co-Authors: Cheng Ning, Hongmei Fang, Yuxiang Tang, Cunliu Zhou

    Abstract:

    Abstract This study aimed to evaluate the effects of l -lysine (Lys)/ l -arginine (Arg)/ l -cysteine (Cys) on the color of cured sausage and the possible mechanism underlying these effects. The results indicated that the combined addition of Arg/Lys/Cys and NaNO2 effectively increased the a* values and nitroso pigment content but decreased the MetMb(Fe3+) content in cured sausage, compared with the individual addition of Arg/Lys/Cys and NaNO2. The cured sausage treated with combined Arg/Lys/Cys and NaNO2 contained significantly lower residual nitrite than those treated with only NaNO2. UV-vis spectroscopy and electron paramagnetic resonance spectroscopy revealed that pentacoordinate nitrosyl ferrohemochrome was the main pigment component in the cured sausage treated with NaNO2 or combined Arg/Lys/Cys and NaNO2 and higher content in the latter one. The results suggest that Arg/Lys/Cys hindered myoglobin oxidation and promoted pentacoordinate nitrosylmyoglobin formation, which could contribute to the improved color of cured sausage. The results are of interest in the meat industry.

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Ioannis A Papayannopoulos – One of the best experts on this subject based on the ideXlab platform.

  • amino acid sequence of a protease inhibitor isolated from sarcophaga bullata determined by mass spectrometry
    Protein Science, 2008
    Co-Authors: Ioannis A Papayannopoulos, Klaus Biemann

    Abstract:

    The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.

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