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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
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Peptides in Brewed Wines: Formation, Structure, and Function.

Mengjie Zhou1, Tingting Bu1, Jiexia Zheng1

  • 1College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou, Zhejiang 310058, People's Republic of China.

Journal of Agricultural and Food Chemistry
|February 23, 2021
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Summary

Peptides in grape wine, Chinese rice wine, and Japanese sake offer health benefits. Further research into their characteristics and mechanisms can unlock their full potential.

Keywords:
Chinese rice winebioactive peptidepeptide formationsakewine

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Area of Science:

  • Food Science
  • Biochemistry
  • Nutritional Science

Background:

  • Traditional low-alcohol beverages like grape wine, sake, and rice wine have global consumption history.
  • Moderate wine consumption is linked to health benefits, though specific components are debated.
  • Peptides are key compounds influencing wine's sensory, technological, and biological properties.

Purpose of the Study:

  • To review the structural and functional characteristics of peptides in grape wine, Chinese rice wine, and Japanese sake.
  • To discuss the formation mechanisms of these peptides.
  • To explore their health-promoting activities and future research directions.

Main Methods:

  • Literature review focusing on scientific studies of peptides in brewed wines.
  • Analysis of existing data on peptide structure, function, and formation.
  • Synthesis of information regarding the physiological activities of wine peptides.

Main Results:

  • Peptides in grape wine, Chinese rice wine, and sake possess diverse structural and functional attributes.
  • Specific formation mechanisms contribute to peptide profiles in these beverages.
  • These peptides exhibit various health-promoting activities, including antioxidant and antimicrobial effects.

Conclusions:

  • Peptides significantly contribute to the desirable attributes of grape wine, Chinese rice wine, and sake.
  • Understanding peptide formation and function is crucial for optimizing wine production and health benefits.
  • Future research should focus on detailed peptide characterization, mechanisms, and physiological actions for targeted applications.