A synthetic conjugate, prepared by covalent binding of a lysozyme fragment (sequence 64-83, denoted "loop" peptide) to a synthetic branched polypeptide, elicited in rabbits the formation of antibodies with specificity directed against a unique region in native lysozyme. These anti-"loop" antibodies were isolated immunospecifically on a lysozyme-cellulose immunoadsorbent. Antibodies with a simil...

Lysozyme was attached to three cotton fabrics through a glycine amino acid linker esterifi ed to cotton cellulose. Lysozyme bound to cotton twill using a carbodiimide-mediated coupling reaction gave the best lysozyme incorporation (16.1 mg/g of cotton). Cotton spunlace nonwoven fabric bound slightly less lysozyme (12.8 mg/g of cotton), but had the best antimicrobial activity. Woven print cloth ...

An oscillating capillary rheometer was used to investigate the effects of xanthan deacetylation on the viscoelastic properties and intrinsic viscosity of xanthan and guar mixtures in dilute aqueous solutions. Deacetylated xanthan exhibited a stronger synergistic interaction with guar than native xanthan did due to the destabilized helical structure and increased chain flexibility of the deacety...

A novel method has been developed for preparing nanogels with a lysozyme core and dextran shell. The method involves the Maillard dry-heat process and heat-gelation process. First, lysozyme-dextran conjugates were produced through the Maillard reaction. Then, the conjugate solution was heated above the denaturation temperature of lysozyme to produce nanogels. The nanogels are of spherical shape...

The xanthan-degrading bacterium Paenibacillus alginolyticus XL-1, isolated from soil, degrades approximately 28% of the xanthan molecule and appears to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including xanthan lyase. Xanthan lyase production was induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation...

Quantitation of lysozyme in human milk was performed by a microparticle-enhanced nephelometric immunoassay based on the measurement of the light scattered during the competitive immunoagglutination of a microparticle-lysozyme conjugate with an anti-lysozyme antiserum. This immunoassay has a detection limit of 8 microg/L of reaction mixture and can be performed using diluted milk (1:6000, in rea...

An oscillating capillary rheometer was used to investigate the dynamic viscoelastic and intrinsic viscosity properties of deacetylated xanthan (0.025%), native xanthan (0.025%), guar gum (0.075%), and xanthan–guar mixtures in dilute solutions. Influence of ionic strength on xanthan conformation and interaction with guar gum was elaborated. As the salt concentration increased, a significant (P <...

Xanthan-modifying enzymes are powerful tools in studying structure-function relationships of this polysaccharide. One of these modifying enzymes is xanthan lyase, which removes the terminal side chain residue of xanthan. In this paper, the cloning and sequencing of the first xanthan lyase-encoding gene is described, i. e., the xalA gene, encoding pyruvated mannose-specific xanthan lyase of Paen...

When the bacterium Bacillus sp. strain GL1 was grown in a medium containing xanthan as the carbon source, the viscosity of the medium decreased in association with growth, showing that the bacterium had xanthan-depolymerizing enzymes. One of the xanthan-depolymerizing enzymes (xanthan lyase) was present in the medium and was found to be induced by xanthan. The xanthan lyase purified from the cu...

Antibodies to nitrotyrosine were prepared in goats or rabbits by injecting a nitrotyrosine-protein conjugate. The antibodies were purified by using a protein that had been nitrated with tetranitromethane. These antibodies were used to isolate nitrotyrosine-containing peptides from nitrated lysozyme. The nitrotyrosine-containing peptides were thus purified (55% yield) in one step and the positio...