Assay of Lysozyme by Its Lytic Action on Leuconostoc Oenos: A Suitable Substrate at Acidic Ph

Pitotti, A.; Bo, A. Dal; Boschelle, O.

doi:10.1111/j.1745-4514.1991.tb00424.x

Cited by 10 publications

(8 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some of the antimicrobial action of eggshell matix proteins could be attributed to the presence of lysozyme; however, it was reported that the minimum inhibition concentration of lysozyme which causes a dramatic decrease in the CFU of St. aureus, was 50 µg/mL (26). The lysozyme concentration in the extracted soluble fraction was estimated to be less than 5% of the total proteins accounted for by enzyme activity test (data not shown) (27), while eggshell matrix proteins exhibited a strong antimicrobial activity in the concentration of 25 µg/mL (the assumed lysozyme concentration with less than 1.25 µg/mL). The present results strongly suggest that eggshell matrix proteins pose novel bactericidal potential in addition to existing lysozyme activity.…”

Section: Resultsmentioning

confidence: 93%

Eggshell Matrix Proteins as Defense Mechanism of Avian Eggs

Mine

Oberle

Kassaify

2002

J. Agric. Food Chem.

View full text Add to dashboard Cite

This study focused on the role of eggshell matrix proteins as a function of potential natural antimicrobial defenses of avian eggs. The electrophoretic profile of SDS-PAGE showed that the soluble eggshell matrix proteins had three major bands of 15 000, 36 000, and 66 000 and several minor bands comprising 17 000, 25 000, 30 000, and 75 000, while insoluble matrix proteins were consisting of various bands comprising at least 16 distinct migration bands between 10 000 and 200 000. Three bacteria species, Pseudomonas aureginosa, Bacillus cereus, and Staphylococcus aureus, were found to be inhibited in the presence of soluble eggshell matrix proteins (100 microg/mL). On the other hand, Escherichia coli and Salmonella enteritidis were weakly inhibited at only an early stage of incubation time (up to 4 h). Scanning electron microscopy revealed that eggshell matrix proteins might interact and disrupt the membrane integrity of bacteria. The present study clearly indicated that avian eggshell matrix proteins possess a potential of novel antimicrobial defensin mechanism.

show abstract

Section: Resultsmentioning

confidence: 93%

Eggshell Matrix Proteins as Defense Mechanism of Avian Eggs

Mine

Oberle

Kassaify

2002

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Lysozyme is a protein with an isoelectric pH of 10.5-11.0 and a molecular mass of about 14 500 Da. Its maximum stability and activity is found at pH values lower than 7.0, namely, in the range of 2.8-4.2, which is the pH range for most wines (7). Lysozyme is available in hydrochloride form, which permits rapid solubility.…”

Section: Introductionmentioning

confidence: 99%

Resistance Screening Essay of Wine Lactic Acid Bacteria on Lysozyme: Efficacy of Lysozyme in Unclarified Grape Musts

Delfini

Cersosimo

Prete

et al. 2004

J. Agric. Food Chem.

View full text Add to dashboard Cite

In wine making, the bacteriolytic activity of lysozyme has primarily been used to control the malolactic fermentation in wines. The use of lysozyme in musts before settling and the beginning of the alcoholic fermentation to inhibit the growth of lactic acid bacteria could be very beneficial. In a resistance test carried out in MT/b broth, lysozyme had greater antimicrobial activity toward Oenococcus oeni than Lactobacillus species. Several strains of wine bacteria belonging to Oenococcus proved sensitive to the bacteriolytic activity of lysozyme at low concentrations in both synthetic medium (MT/b) (50 mg/L), white must, or red must made with or without the skins (100 mg/L). Lactobacillus and Pediococcus strains survived at lysozyme concentrations of 200-500 and 500 mg/L, respectively, in MT/b and musts. Suspended solids in unclarified musts may strongly bind to lysozyme thereby causing its removal by filtration or centrifugation. One hour after lysozyme was added to musts, it was quantified by HPLC and found after centrifugation to be 40-50% and only 10% in musts made with or without the skins, respectively. Although appreciable amounts of lysozyme were bound to wine components, this did not appear to be a serious hindrance to lysozyme activity.

show abstract

“…Lysozyme helps control nralolactic fermentation (MLF) in wine by limiting LAB proliferation (3,6,30,42). Lysozyme is not affected by alcohol and is active in the pH range (3 to 4) of the winemaking process (9,43), with no effect on the organoleptic quality of wine (11,17). In addition, this protein does not enhance the browning of white wines during their storage (5), and its activity is not significantly influenced by the most common technological processes used in winemaking (1).…”

mentioning

confidence: 97%

Antibacterial Activity of Hen Egg White Lysozyme Modified by Heat and Enzymatic Treatments against Oenological Lactic Acid Bacteria and Acetic Acid Bacteria

Carrillo

García-Ruiz

Recio

et al. 2014

Journal of Food Protection

View full text Add to dashboard Cite

The antimicrobial activity of heat-denatured and hydrolyzed hen egg white lysozyme against oenological lactic acid and acetic acid bacteria was investigated. The lysozyme was denatured by heating, and native and heat-denatured lysozymes were hydrolyzed by pepsin. The lytic activity against Micrococcus lysodeikticus of heat-denatured lysozyme decreased with the temperature of the heat treatment, whereas the hydrolyzed lysozyme had no enzymatic activity. Heat-denatured and hydrolyzed lysozyme preparations showed antimicrobial activity against acetic acid bacteria. Lysozyme heated at 90°C exerted potent activity against Acetobacter aceti CIAL-106 and Gluconobacter oxydans CIAL-107 with concentrations required to obtain 50% inhibition of growth (IC50) of 0.089 and 0.013 mg/ml, respectively. This preparation also demonstrated activity against Lactobacillus casei CIAL-52 and Oenococcus oeni CIAL-91 (IC50, 1.37 and 0.45 mg/ml, respectively). The two hydrolysates from native and heat-denatured lysozyme were active against O. oeni CIAL-96 (IC50, 2.77 and 0.3 mg/ml, respectively). The results obtained suggest that thermal and enzymatic treatments increase the antibacterial spectrum of hen egg white lysozyme in relation to oenological microorganisms.

show abstract

Assay of Lysozyme by Its Lytic Action on Leuconostoc Oenos: A Suitable Substrate at Acidic Ph

Cited by 10 publications

References 7 publications

Eggshell Matrix Proteins as Defense Mechanism of Avian Eggs

Eggshell Matrix Proteins as Defense Mechanism of Avian Eggs

Resistance Screening Essay of Wine Lactic Acid Bacteria on Lysozyme: Efficacy of Lysozyme in Unclarified Grape Musts

Antibacterial Activity of Hen Egg White Lysozyme Modified by Heat and Enzymatic Treatments against Oenological Lactic Acid Bacteria and Acetic Acid Bacteria

Contact Info

Product

Resources

About