scholarly journals Distinct pathways for modification of the bacterial cell wall by non-canonicalD-amino acids

2011 ◽  
Vol 30 (16) ◽  
pp. 3442-3453 ◽  
Author(s):  
Felipe Cava ◽  
Miguel A de Pedro ◽  
Hubert Lam ◽  
Brigid M Davis ◽  
Matthew K Waldor
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall

Synthesis of modified partial structures of the bacterial cell wall. 1. Lipopeptides containing nonproteinogenic amino acids

1993 ◽  
Vol 58 (3) ◽  
pp. 683-689 ◽  
Author(s):  
Helmut Schneider ◽  
Gerhard Sigmund ◽  
Bettina Schricker ◽  
Klaus Thirring ◽  
Heinz Berner
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Partial Structures

scholarly journals Preservation of amino acids from in situ-produced bacterial cell wall peptidoglycans in northeastern Atlantic continental margin sediments

2002 ◽  
Vol 47 (5) ◽  
pp. 1521-1524 ◽  
Author(s):  
Mark Grutters ◽  
Wim van Raaphorst ◽  
Eric Epping ◽  
Willem Helder ◽  
Jan W. de Leeuw ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Continental Margin ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Northeastern Atlantic

scholarly journals Lysozyme from Chicken Egg White as an Antibacterial Agent

2019 ◽  
Vol 28 (4) ◽  
pp. 175
Author(s):  
Harsi Dewantari Kusumaningrum ◽  
Syahrizal Nasution ◽  
E Kusumaningtyas ◽  
D N Faridah
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Antibacterial Activity ◽  
Bacterial Cell ◽  
Egg White ◽  
Bacterial Cell Wall ◽  
Enzymatic Treatment ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Chicken Egg

<p class="00-6Abstrak2Wtz">Lysozyme is one of the constituent proteins of chicken egg white that plays an important role in a protection system during the embryo growing process. Lysozyme protection systems can be applied in food and for health. This paper aims to describe the role of egg white lysozyme which has the antibacterial activity to improve food safety and health. Mechanism and activity of lysozyme protection can be explored by understanding the structure of proteins, type of amino acids, and the sequence of amino acids. The mechanism of lysozyme antibacterial activity against Gram positive bacteria occurs through its ability to breakdown the peptidoglycan glycosidic bonds in the bacterial cell wall membrane. The antibacterial activity of lysozyme can be increased when its normal lysozyme form was denatured/hydrolyzed through modifying the lysozyme structure by heat and enzymatic treatment. Heat treatment will reveal the active site of lysozyme after denaturation, leading to the destruction of the bacterial cell wall membrane. Enzymatic treatment through hydrolysis process of hydrolysis by protease enzymes will generate antibacterial peptides, which have the ability to inhibit the growth of Gram positive bacteria and Gram negative bacteria. Antibacterial lysozyme peptides and heat treated lysozyme are dominated by hydrophobic amino acids and positively charged to facilitate interaction between lysozyme and lipopolysaccharide which coats peptidoglycan. Antibacterial lysozyme peptide can be used as an antibiotic and a safe natural preservative compared to synthetic material and can reduce the risk of destructive bacteria and pathogenic bacteria. Lysozyme peptide is potential to protect human health since it has also other activities such as inhibition of angiotensin-converting enzyme, antihypertensive, antitumor, antioxidant, and antiviral agents.</p>

ChemInform Abstract: Synthesis of Modified Partial Structures of the Bacterial Cell Wall. Part 1. Lipopeptides Containing Nonproteinogenic Amino Acids.

ChemInform ◽  
2010 ◽  
Vol 24 (32) ◽  
pp. no-no
Author(s):  
H. SCHNEIDER ◽  
G. SIGMUND ◽  
B. SCHRICKER ◽  
K. THIRRING ◽  
H. BERNER
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Partial Structures

scholarly journals Viral lysis of bacteria: an important source of dissolved amino acids and cell wall compounds

2006 ◽  
Vol 86 (3) ◽  
pp. 605-612 ◽  
Author(s):  
Mathias Middelboe ◽  
Niels O.G. Jørgensen
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Organic Matter ◽  
Organic Carbon ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Diaminopimelic Acid ◽  
Wall Material ◽  
Cell Wall Material ◽  
Viral Lysis

Viral infection of bacteria causes release of dissolved organic matter (DOM), which is available for bacterial uptake. In aquatic environments, this virus-mediated transformation of living cells into dissolved and colloidal organic matter may be a quantitatively important process in the pelagic recycling of carbon and nutrients, but little is known about the amount, composition, or bioavailability of viral lysates. By using a model system of a marine bacterium (Cellulophaga sp.) and a virus specific to this bacterium, the present study provides a first quantification of the input of dissolved free and combined amino acids (DFAA and DCAA) and bacterial cell wall compounds following viral lysis. The DCAA constituted 51–86% of the total virus-mediated organic carbon release of 1087–1825 μg C l−1 (estimated biomass of the lysed bacteria), whereas DFAA and glucosamine each accounted for 2–3% of total lysate-C. The viral particles themselves constituted 4–6% of the released organic carbon, and altogether, the applied analyses thus identified 53–92% of the released lysates. Approximately 12% of the identified compounds were derived from bacterial cell wall peptidoglycan, including various D-isomers of DFAA and DCAA, glucosamine and diaminopimelic acid (DAPA). Although a portion of this cell wall material may have entered the pool of refractory material, a significant fraction of some peptidoglycan-derived components, e.g. 83% of the released D-DFAA, were removed from the dissolved phase during the last part of the incubations, suggesting that part of the cell wall material were utilized by the developing virus-resistant Cellulophaga population. Therefore, we suggest that virus-mediated DOM is a source of a variety of organic compounds, which contribute significantly to the pool of rapidly recycling material in the ocean.

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