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  1. Recovery of value-added glycopeptides from edible bird's nest (EBN) co-products: enzymatic hydrolysis, physicochemical characteristics and bioactivity
    Ling JWA, Chang LS, Babji AS, Lim SJ
    J Sci Food Agric, 2020 Oct;100(13):4714-4722.
    PMID: 32468613 DOI: 10.1002/jsfa.10530
    BACKGROUND: Processing of edible bird's nest (EBN) requires extensive washing to remove impurities and produces huge amounts of EBN co-products, which contain mainly feathers with glycoproteins attached, which are usually discarded. This study was conducted to recover the valuable EBN glycoproteins from the waste material. Enzymatic hydrolysis was applied to recover EBN glycopeptides from EBN co-products (EBNcoP ) and processed cleaned EBN (EBNclean ) was used as control, which were then freeze-dried into EBN hydrolysates (EBNhcoP and EBNhclean , respectively).

    RESULTS: The recovery yield for EBNhclean and EBNhcoP were 89.09 ± 0.01% and 47.64 ± 0.26%, respectively, indicating nearly 50% of glycopeptide can be recovered from the waste material. Meanwhile, N-acetylneuraminic acid, a major acid sugar in EBN glycoproteins, of EBNhcoP increased by 229% from 58.6 ± 3.9 to 192.9 ± 3.1 g kg-1 , indicating the enzymatic hydrolysis removed impurities and thus enhanced the N-acetylneuraminic acid content. Total soluble protein was more than 330 g kg-1 for all the samples. Colour parameter showed that hydrolysate samples have greater L* (lightness) values. Chroma result indicates the intensity of all the samples were low (

    Matched MeSH terms: Glycopeptides/chemistry*
  2. Oritavancin - a new semisynthetic lipoglycopeptide agent to tackle the challenge of resistant gram positive pathogens
    Das B, Sarkar C, Schachter J
    Pak J Pharm Sci, 2013 Sep;26(5):1045-55.
    PMID: 24035967
    Natural glycopeptide antibiotics like vancomycin and teicoplanin have played a significant role in countering the threat posed by Gram-positive bacterial infections. The emergence of resistance to glycopeptides among enterococci and staphylococci has prompted the search for second-generation drugs of this class and semi-synthetic derivatives are currently under clinical trials. Antimicrobial resistance among Gram-positive organisms has been increasing steadily during the past several decades and the current development of antibiotics falls short of meeting the needs. Oritavancin (LY-333328 diphosphate), a promising novel second-generation semisynthetic lipoglycopeptide, has a mechanism of action similar to that of other glycopeptides. It has concentration-dependent activity against a variety of Gram-positive organisms specially methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-intermediate resistant Staphylococcus aureus (VISA), Streptococcus pneumoniae and vancomycin-resistant enterococcus. It is rapidly bactericidal against many species and in particular for enterococci where vancomycin and teicoplanin are only bacteriostatic even against susceptible strains. The pharmacokinetic profile of oritavancin has not been fully described; however, oritavancin has a long half-life of about 195.4 hours and is slowly eliminated by renal means. Oritavancin is not metabolized by the liver in animals. Oritavancin will most probably be prescribed as a once-daily dose and it demonstrates concentration-dependent bactericidal activity. Oritavancin has demonstrated preliminary safety and efficacy in Phase I and II clinical trials. In a Phase III clinical trial, oritavancin has achieved the primary efficacy end point in the treatment of complicated Gram-positive skin and skin-structure infections. To date, adverse events have been mild and limited; the most common being administration site complaints, headache, rhinitis, dry skin, pain, increases in liver transaminases and accumulation of free cholesterol and phospholipids in phagocytic (macrophages) and nonphagocytic (fibroblast) cells. Oritavancin appears to be a promising antimicrobial alternative to vancomycin (with additional activity against Staphylococcus and Enterococcus resistant to vancomycin) for the treatment of complicated Gram-positive skin and skin-structure infections. Additional clinical data are required to fully explore its use.
    Matched MeSH terms: Glycopeptides/chemistry
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