Kinetic modeling of thermal inactivation of antimicrobial peptides produced by Lactobacillus sakei subsp. sakei 2a

2015 ◽  
Vol 605 ◽  
pp. 95-99 ◽  
Author(s):  
Patrícia da Silva Malheiros ◽  
Voltaire Sant ◽  
Adriano Brandelli ◽  
Bernadette Dora Gombossy de Melo Franco
Keyword(s):  
Antimicrobial Peptides ◽  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Lactobacillus Sakei

Kinetic Modeling of the Thermal Inactivation of Bacteriocin-Like Inhibitory Substance P34

2010 ◽  
Vol 58 (5) ◽  
pp. 3147-3152 ◽  
Author(s):  
Voltaire Sant’Anna ◽  
Michele Utpott ◽  
Florencia Cladera-Olivera ◽  
Adriano Brandelli
Keyword(s):  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Inhibitory Substance

Immobilization of antimicrobial peptides from Lactobacillus sakei subsp. sakei 2a in bacterial cellulose: Structural and functional stabilization

2018 ◽  
Vol 17 ◽  
pp. 25-29 ◽  
Author(s):  
Patrícia S. Malheiros ◽  
Angela F. Jozala ◽  
Adalberto Pessoa-Jr. ◽  
Marta M.D.C. Vila ◽  
Victor M. Balcão ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Bacterial Cellulose ◽  
Lactobacillus Sakei

Kinetic modeling of thermal inactivation of the Bacillus sp. protease P7

2012 ◽  
Vol 36 (7) ◽  
pp. 993-998 ◽  
Author(s):  
Voltaire Sant’Anna ◽  
Ana Paula Folmer Corrêa ◽  
Daniel Joner Daroit ◽  
Adriano Brandelli
Keyword(s):  
Kinetic Modeling ◽  
Thermal Inactivation ◽  
Bacillus Sp

Allene oxidation in jet-stirred reactor : a kinetic modeling study

1990 ◽  
Vol 87 ◽  
pp. 1159-1172 ◽  
Author(s):  
P Dagaut ◽  
M Cathonnet ◽  
B Aboussi ◽  
JC Boettner
Keyword(s):  
Kinetic Modeling ◽  
Stirred Reactor ◽  
Allene Oxidation ◽  
Modeling Study

Antimicrobial peptides in COPD

Pneumologie ◽  
2009 ◽  
Vol 63 (S 01) ◽  
Author(s):  
G Günther ◽  
E Andresen ◽  
J Bullwinkel ◽  
C Lange ◽  
H Heine
Keyword(s):  
Antimicrobial Peptides

Mechanism of Inhibitory Action on Platelet Activation of a Phospholipase A2 Isolated from Lachesis muta (Bushmaster) Snake Venom

1997 ◽  
Vol 78 (05) ◽  
pp. 1372-1380 ◽  
Author(s):  
André L Fuly ◽  
Olga L T Machado ◽  
Elias W Alves ◽  
Célia R Carlinis
Keyword(s):  
Platelet Aggregation ◽  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Inhibitory Activity ◽  
Thermal Inactivation ◽  
Anticoagulant Activity ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Crude Venom ◽  
Lachesis Muta

SummaryCrude venom from Lachesis muta exhibited procoagulant, proteolytic and phospholipase A2 activities. A phospholipase A2, denoted LM-PLA2 was purified from L. muta venom to homogeneity, through a combination of chromatographic steps involving gel-filtration on Sephacryl S-200 HR and reverse phase chromatography on a C2/C18 column. LM-PLA2 presented a single polypeptide chain with an isoelectric point at pH 4.7 and apparent molecular weight of 17 kDa. Partial aminoacid sequence indicated a high degree of homology for LM-PLA2 with other PLA2 from different sources.LM-PLA2 displayed a potent enzymatic activity as measured by indirect hemolysis of red blood cells but it was neither lethal when injected i.p. into mice nor did it present anticoagulant activity. Furthermore, LM-PLA2 displayed a moderate inhibitory activity on the aggregation of rabbit platelets induced by low levels of ADP, thrombin and arachidonate. In contrast, platelet aggregation induced by high doses of collagen was strongly inhibited by LM-PLA2 as well as ATP-release. Treatment of the protein with p-bromophenacyl bromide or 2-mercapto-ethanol, as well as thermal inactivation studies, suggested that the platelet inhibitory effect of LM-PLA2 is dependent on its enzymatic activity. Thus, the platelet inhibitory activity of LM-PLA2 was shown to be dependent on the hydrolysis of plasma phospholipids and/or lipoproteins, most probably those rich in phosphatidylcholine. Surprisingly, lyso-phosphatidylcholine released by LM-PLA2 from plasma was shown to preferentially inhibited collagen-induced platelet aggregation, in contrast to other PLA2s, whose plasma hydrolytic products indistinctly affect platelet’s response to several agonists.

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