Efficacy of a lactylate on production performance and intestinal health of broilers during a subclinical Clostridium perfringens infection.

Clostridium perfringens, an α-toxin producing gram-positive bacterium, is an enteric pathogen for poultry. Because subclinical C. perfringens infections often result in damage of the intestinal mucosa, decreased nutrient digestion, and poor performance, efforts should be taken to find an effective strategy that controls overgrowth of C.

Promicromonospora pachnodae sp. nov., a member of the (hemi)cellulolytic hindgut flora of larvae of the scarab beetle Pachnoda marginata.

Intestinal microorganisms play an important role in plant fiber degradation by larvae of the rose chafer Pachnoda marginata. In the hindgut of the larvae 2.5 to 7.

Effect of sporulation and recovery medium on the heat resistance and amount of injury of spores from spoilage bacilli.

Aims: To assess the influence of sporulation media on heat resistance, and the use of stress recovery media to measure preservation injury of spores of five representative spoilage bacilli.

Methods And Results: Bacillus spores prepared on nutrient agar supplemented with Ca2+, Mg2+, Mn2+, Fe2+ and K+ were more heat-resistant than spores obtained from nutrient agar with Mn2+. This increased heat resistance correlated with a decrease in the protoplast water content as determined by buoyant density sedimentation.

A beta-1,4-endoglucanase-encoding gene from Cellulomonas pachnodae.

A gene library of Cellulomonas pachnodae was constructed in Escherichia coli and was screened for endoglucanase activity. Five endoglucanase-positive clones were isolated that carried identical DNA fragments. The gene, designated cel6A, encoding an endoglucanase enzyme, belongs to the glycosyl hydrolase family 6 (cellulase family B).

Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae.

Two xylanase-encoding genes, named xyn11A and xyn10B, were isolated from a genomic library of Cellulomonas pachnodae by expression in Escherichia coli. The deduced polypeptide, Xyn11A, consists of 335 amino acids with a calculated molecular mass of 34,383 Da. Different domains could be identified in the Xyn11A protein on the basis of homology searches.