Table 5. Enzymatic sensitivity and heat stability profile of antimicrobial activities.
Isolate | Activity* | Proteinase K (proK) | Pronase E (proE) | Trypsin | Lipase | Sensitive to enzymes | Resistant to (t °C) |
---|---|---|---|---|---|---|---|
#01 | 13.67 ± 0.58 | 10.67 ± 0.58 | 10.67 ± 0.58 | 14.00 | 13.67 ± 0.58 | proE, proK | 60 |
#02 | 11.00 | 9.00 | – | 10.67 ± 0.58 | 11.00 | proE, proK | 60 |
#04 | 9.00 | – | – | – | 9.00 | proE, proK, trypsin | – |
#05 | 23.67 ± 0.58 | 23.67 ± 0.58 | 23.67 ± 0.58 | 23.67 ± 0.58 | 23.67 ± 0.58 | – | 60 |
#06 | 14.67 ± 0.58 | 13.00 ± 1.00 | 10.33 ± 0.58 | – | – | proE, trypsin, lipase | – |
#08 | 13.67 ± 0.58 | 12.00 | 11.33 ± 0.33 | 13.33 ± 0.33 | 14.00 | proE, proK | 60 |
#10 | 9.00 | – | – | – | 9.00 | proE, proK, trypsin | – |
#11 | 17.00 | 15.00 | – | 15 ± 0.58 | – | proE, proK, lipase | 60 |
#12 | 11.67 ± 0.58 | 8.67 ± 0.58 | – | – | 12.00 | proE, proK, trypsin | – |
#13 | 16.00 | 16.00 | 16.00 | 12.57 ± 0.58 | 18.33 ± 0.58 | trypsin | 60 |
#14 | 8.67 ± 0.58 | 8.67 ± 0.58 | – | – | – | proE, proK, trypsin, lipase | – |
#15 | 8.67 ± 0.58 | – | – | 9.00 | 9.00 | proE, trypsin | – |
#16 | 12.00 ± 0.58 | – | – | – | 12.00 | proE, proK, trypsin | – |
#17 | 12.33 ± 0.58 | 9.67 ± 0.58 | – | – | 8.67 ± 0.58 | proE, proK, trypsin | – |
#18 | 9.67 ± 0.58 | 10.33 ± 0.58 | 10.00 | 10.33 ± 0.58 | 10.00 | – | – |
#19 | 13.67 ± 0.58 | 14.00 | 13.67 ± 0.58 | 13.67 ± 0.58 | 12.67 ± 0.58 | – | 60 |
#20 | 11.00 | 11.00 | 8.67 ± 0.58 | 11.00 | 11.00 | proE | – |
#21 | 15.00 | 11.00 | 12.33 ± 0.58 | 15.00 | 11.33 ± 0.58 | proE, proK, lipase | – |
#23 | 13.00 | 12.33 ± 0.58 | – | 12.33 ± 0.58 | 12.67 ± 0.58 | proE | – |
Notes.
Value indicated the diameter of halo zone of antimicrobial activity in millimetres including well diameter of 6 mm
indicates no zone of clearing.
Underlined enzyme indicated a loss of activity after enzymatic treatment. The values of temperature resistance were recorded after 3 hours of incubation. The numbers in the table represented the mean value (±standard deviation) of killing diameters from the measurement of three replicates. These 19 isolates showed antagonistic activities against Clostridium perfringens.