Thermal inactivation of actinidin as affected by meat matrix

Meat Science ◽  
2018 ◽  
Vol 145 ◽  
pp. 238-244 ◽  
Author(s):  
Xiaojie Zhu ◽  
Lovedeep Kaur ◽  
Mike Boland
Keyword(s):  
Thermal Inactivation ◽  
Meat Matrix

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.

scholarly journals Thermal Inactivation of Susceptible and Multiantimicrobial-Resistant Salmonella Strains Grown in the Absence or Presence of Glucose

2003 ◽  
Vol 69 (7) ◽  
pp. 4123-4128 ◽  
Author(s):  
R. T. Bacon ◽  
J. R. Ransom ◽  
J. N. Sofos ◽  
P. A. Kendall ◽  
K. E. Belk ◽  
...  
Keyword(s):  
Heat Stress ◽  
Protective Effect ◽  
Thermal Tolerance ◽  
Thermal Inactivation ◽  
Survival Curves ◽  
Acid Adaptation ◽  
Circulating Water ◽  
Glucose Levels ◽  
Study Results ◽  
Peptone Water

ABSTRACT The heat resistance of susceptible and multiantimicrobial-resistant Salmonella strains grown to stationary phase in glucose-free tryptic soy broth supplemented with 0.6% yeast extract (TSBYE−G; nonadapted), in regular (0.25% glucose) TSBYE, or in TSBYE−G with 1.00% added glucose (TSBYE+G; acid adapted) was determined at 55, 57, 59, and 61°C. Cultures were heated in sterile 0.1% buffered peptone water (50 μl) in heat-sealed capillary tubes immersed in a thermostatically controlled circulating-water bath. Decimal reduction times (D values) were calculated from survival curves having r 2 values of >0.90 as a means of comparing thermal tolerance among variables. D 59°C values increased (P < 0.05) from 0.50 to 0.58 to 0.66 min for TSBYE−G, TSBYE, and TSBYE+G cultures, respectively. D 61°C values of antimicrobial-susceptible Salmonella strains increased (P < 0.05) from 0.14 to 0.19 as the glucose concentration increased from 0.00 to 1.00%, respectively, while D 61°C values of multiantimicrobial-resistant Salmonella strains did not differ (P > 0.05) between TSBYE−G and TSBYE+G cultures. When averaged across glucose levels and temperatures, there were no differences (P > 0.05) between the D values of susceptible and multiantimicrobial-resistant inocula. Collectively, D values ranged from 4.23 to 5.39, 1.47 to 1.81, 0.50 to 0.66, and 0.16 to 0.20 min for Salmonella strains inactivated at 55, 57, 59, and 61°C, respectively. zD values were 1.20, 1.48, and 1.49°C for Salmonella strains grown in TSBYE+G, TSBYE, and TSBYE−G, respectively, while the corresponding activation energies of inactivation were 497, 493, and 494 kJ/mol. Study results suggested a cross-protective effect of acid adaptation on thermal inactivation but no association between antimicrobial susceptibility and the ability of salmonellae to survive heat stress.

scholarly journals Degradation of keratan sulphate by β-N-acetylhexosaminidases A and B

1981 ◽  
Vol 193 (3) ◽  
pp. 811-818 ◽  
Author(s):  
T Ludolph ◽  
E Paschke ◽  
J Glössl ◽  
H Kresse
Keyword(s):  
Isoelectric Focusing ◽  
Human Liver ◽  
Thermal Inactivation ◽  
Sandhoff Disease ◽  
Chromogenic Substrate ◽  
Polymeric Substrate ◽  
Keratan Sulphate ◽  
Human Enzyme ◽  
Tay Sachs Disease

Enzymic cleavage of beta-N-acetylglucosamine residues of keratan sulphate was studied in vitro by using substrate a [3H]glucosamine-labelled desulphated keratan sulphate with N-acetylglucosamine residues at the non-reducing end. Both lysosomal beta-N-acetylhexosaminidases A and B are proposed to participate in the degradation of keratan sulphate on the basis of the following observations. Homogenates of fibroblasts from patients with Sandhoff disease, but not those from patients with Tay–Sachs disease, were unable to release significant amounts of N-acetyl[3H]glucosamine. On isoelectric focusing of beta-N-acetylhexosaminidase from human liver the peaks of keratan sulphate-degrading activity coincided with the activity towards p-nitrophenyl beta-N-acetylglucosaminide. A monospecific antibody against the human enzyme reacted with both enzyme forms and precipitated the keratan sulphate-degrading activity. Both isoenzymes had the same apparent Km of 4mM, but the B form was approximately twice as active as the A form when compared with the activity towards a chromogenic substrate. Differences were noted in the pH–activity profiles of both isoenzymes. Thermal inactivation of isoenzyme B was less pronounced towards the polymeric substrate than towards the p-nitrophenyl derivative.

Methods to obtain thermal inactivation data for pathogen control in low-moisture foods

2021 ◽  
Vol 112 ◽  
pp. 174-187
Author(s):  
Teng Cheng ◽  
Juming Tang ◽  
Ren Yang ◽  
Yucen Xie ◽  
Long Chen ◽  
...  
Keyword(s):  
Thermal Inactivation ◽  
Pathogen Control ◽  
Low Moisture Foods

scholarly journals Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E

2021 ◽  
Vol 85 (2) ◽  
pp. 386-390
Author(s):  
Manami Suzuki ◽  
Teisuke Takita ◽  
Kohei Kuwata ◽  
Kota Nakatani ◽  
Tongyang Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Thermodynamic Analysis ◽  
Thermal Inactivation ◽  
Entropy Change ◽  
Crystallographic Analysis ◽  
Bacillus Sp ◽  
Amino Acid Residues ◽  
Gh10 Xylanase ◽  
Insight Into

ABSTRACT The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.

Modeling the Effects of Temperature, Sodium Chloride, and Green Tea and Their Interactions on the Thermal Inactivation of Listeria monocytogenes in Turkey†

2014 ◽  
Vol 77 (10) ◽  
pp. 1696-1702 ◽  
Author(s):  
VIJAY K. JUNEJA ◽  
JIMENA GARCIA-DÁVILA ◽  
JULIO CESAR LOPEZ-ROMERO ◽  
ETNA AIDA PENA-RAMOS ◽  
JUAN PEDRO CAMOU ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Sodium Chloride ◽  
Protective Effect ◽  
Heat Resistance ◽  
Green Tea ◽  
Thermal Inactivation ◽  
Heating Temperature ◽  
Lethal Effect ◽  
Interactive Effects ◽  
D Values

The interactive effects of heating temperature (55 to 65°C), sodium chloride (NaCl; 0 to 2%), and green tea 60% polyphenol extract (GTPE; 0 to 3%) on the heat resistance of a five-strain mixture of Listeria monocytogenes in ground turkey were determined. Thermal death times were quantified in bags that were submerged in a circulating water bath set at 55, 57, 60, 63, and 65°C. The recovery medium was tryptic soy agar supplemented with 0.6% yeast extract and 1% sodium pyruvate. D-values were analyzed by second-order response surface regression for temperature, NaCl, and GTPE. The data indicated that all three factors interacted to affect the inactivation of the pathogen. The D-values for turkey with no NaCl or GTPE at 55, 57, 60, 63, and 65°C were 36.3, 20.8, 13.2, 4.1, and 2.9 min, respectively. Although NaCl exhibited a concentration-dependent protective effect against heat lethality on L. monocytogenes in turkey, addition of GTPE rendered the pathogen more sensitive to the lethal effect of heat. GTPE levels up to 1.5% interacted with NaCl and reduced the protective effect of NaCl on heat resistance of the pathogen. Food processors can use the predictive model to design an appropriate heat treatment that would inactivate L. monocytogenes in cooked turkey products without adversely affecting the quality of the product.

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