Autolytic Activity (autolytic + activity)

Distribution by Scientific Domains


Selected Abstracts


Autolytic phenotype of Lactococcus lactis strains isolated from traditional Tunisian dairy products

JOURNAL OF APPLIED MICROBIOLOGY, Issue 5 2002
H. Ouzari
Aims:,To evaluate the autolytic properties of Lactococcus lactis strains isolated from artisan Tunisian dairy products, their peptidoglycan hydrolase content and their activity spectrum. Methods and Results:,The autolytic phenotype of Lactococcus strains was evaluated under starvation conditions in potassium phosphate buffer. The results obtained highlighted a high degree of diversity among the strains analysed, allowing the identification of high and low autolytic Lactococcus lactis strains. Peptidoglycan hydrolase content was evaluated by renaturing SDS-PAGE using cells of Micrococcus lysodeikticus as a target for the enzymatic activity. A major activity band migrating at about 45 kDa was observed. The lytic activity, evaluated in the presence of different chemicals, was retained in 8% NaCl, 15 mmol l,1 CaCl2, and in a pH range between 5 and 9·5. The substrate specificity of peptidoglycan hydrolase from Lactococcus strains was evaluated in renaturing SDS-PAGE incorporating cells of different bacterial species. The major autolysin of Lactococcus lactis was active against cells of Lactococcus lactis subsp. lactis, Streptococcus thermophilus, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus helveticus and Listeria monocytogenes. Conclusions:,Autolytic activity is widely distributed in Lactococcus lactis and the rate of autolysis is strain-dependent. The major peptidoglycan hydrolase showed a wide spectrum of activity against several lactic acid bacteria and bacterial species involved in food-related infection. Significance and Impact of the Study:,The autolytic phenotype of Lactococcus lactis strains isolated from Tunisian artisan dairy products has been determined, and the data obtained should allow the selection of strains of technological interest in the cheese-ripening process. [source]


Functional and Thermal Gelation Properties of Squid Mantle Proteins Affected by Chilled and Frozen Storage

JOURNAL OF FOOD SCIENCE, Issue 6 2003
M.C. Gómez-Guillén
ABSTRACT: Fresh squid (Loligo vulgaris) mantles that underwent chilled and frozen storage were studied for their ability to form thermal gels as well as the effects of changes to the functional and chemical properties of the muscle proteins during storage. Assays of protein extractability in 5% NaCl, apparent viscosity, autolytic activity, and SDS-PAGE (of the soluble fraction) were carried out periodically. After 4 d of chilled storage, there was a significant drop in protein functionality that negatively affected the thermal gelation profile. The rate of proteolysis remained very high throughout frozen storage, however functional properties and thermal behavior remained very stable. [source]


Porcine Plasma Proteins as a Surimi Protease Inhibitor: Effects on Actomyosin Gelation

JOURNAL OF FOOD SCIENCE, Issue 4 2000
W. Visessanguan
ABSTRACT Effect of porcine plasma proteins (PPP) on thermal gelation of actomyosin in the presence and absence of fish proteinase was studied using a dynamic rheological test. Substantial decreases in development rate and magnitude of gel modulus were observed by the addition of proteinase to actomyosin gels. PPP was effective in protecting a myosin-heavy chain from proteolytic degradation, however, PPP itself interfered with the formation of actomyosin gel. Lower gel modulus was observed with actomyosin gels developed with higher concentrations of PPP added. Overall, PPP reversed the loss of gel modulus by the proteinase, however, the recovered gel modulus was only as high as those containing PPP only. These results implicated that, although PPP may revert autolytic activity in surimi, it interfaces with actomyosin gelation. [source]


Characterization of RAT, an autolysis regulator in Staphylococcus aureus

MOLECULAR MICROBIOLOGY, Issue 6 2003
S. S. Ingavale
Summary In trying to identify genetic loci involved in the regulation of cap5 genes in Staphylococcus aureus, we isolated a transposon mutant that exhibited a growth defect, enhanced autolysis and increased sensitivity to Triton X-100 and penicillin, attributable in part to increased murein hydrolase activity. Analysis of the chromosomal sequence flanking the transposon insertion site revealed that the gene disrupted in the mutant encodes an open reading frame of 147 amino acids. We named this gene rat, which stands for regulator of autolytic activity. Sequence analysis indicated that Rat is homologous to the MarR and, to a lesser extent, the SarA protein families. Mutations in rat resulted in decreased expression of known autolytic regulators lytSR, lrgAB and arlRS. Gel shift studies indicated that Rat binds to the lytRS and arlRS promoters, thus confirming Rat as a DNA-binding protein to these known repressors of autolytic activity. As anticipated, rat appears to be a negative regulator of autolysin genes including lytM and lytN. These data suggest that the rat gene product is an important regulator of autolytic activity in S. aureus. [source]