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Table 1 Effect of some additives, substrate chain length and temperature on the activity of LipC12

From: Identification and characterization of a new true lipase isolated through metagenomic approach

Variable

Relative

Variable

Relative

Variable

Relative

 

activity (%)

 

activity (%)

 

activity (%)

Cation (1 mM) after EDTA chelationa

Cation (1 mM) without EDTA chelation

Substrate specificity

   None

   < 0.5

   Noneb

   100.0 ± 3.4

   pNP palmitate (C16:0)b,d

   100.0 ± 2.2

   CaCl2b

   100.0 ± 1.2

   RbCl

   128.4 ± 2.3

   pNP myristate (C14:0)

   75.4 ± 1.7

   CuCl2

   59.3 ± 0.3

   KCl

   121.8 ± 4.6

   pNP dodecanoate (C12:0)

   90.0 ± 4.9

   Al2(SO4)3

   59.2 ± 0.1

   CsCl

   104.1 ± 4.7

   pNP decanoate (C10:0)

   83.2 ± 1.7

   CoCl2

   54.9 ± 0.6

   NaCl

   94.3 ± 4.4

   pNP caproate (C6:0)

   29.3 ± 0.7

   MnCl2

   54.9 ± 1.2

   LiCl

   92.7 ± 2.3

   pNP valerate (C5:0)

   34.3 ± 2.1

   NiCl2

   53.3 ± 0.6

   Ba(Ac)2

   85.4 ± 5.3

   pNP butyrate (C4:0)

   25.6 ± 0.8

   FeSO4

   37.4 ± 0.9

   CaCl2

   73.4 ± 4.2

   pNP acetate (C2:0)

   1.9 ± 0.2

   Pb(Ac)2

   33.9 ± 0.2

   SnCl2

   67.6 ± 3.4

Optimal temperature e

 

   CdSO4

   32.7 ± 0.3

   NiCl2

   66.0 ± 1.0

   9.9°C

   38.4 ± 6.4

   HgCl2

   29.5 ± 0.9

   MgCl2

   64.5 ± 1.9

   20.5°C

   93.8 ± 6.6

   MgCl2

   4.0 ± 0.1

   HgCl2

   62.3 ± 1.3

   30.0°Cb

   100.0 ± 5.1

   AgNO3

   0.9 ± 0.2

   CoCl2

   53.8 ± 0.7

   40.0°C

   37.7 ± 7.7

   Ba(Ac)2

   0.8 ± 0.1

   CuCl2

   52.4 ± 0.9

   50.7°C

   14.8 ± 3.5

   KCl

   < 0.5

   CdSO4

   49.8 ± 2.3

   60.6°C

   11.1 ± 3.6

   ZnCl2

   < 0.5

   FeCl3

   48.8 ± 5.3

Sodium chloride

   SnCl2

   < 0.5

   MnCl2

   47.1 ± 1.7

   Noneb

   100.0 ± 2.9

   LiCl

   < 0.5

   ZnCl2

   44.5 ± 2.9

   0.01 M

   109.4 ± 4.5

   RbCl

   < 0.5

   Al2(SO4)3

   44.8 ± 1.3

   0.05 M

   121.8 ± 2.0

   CsCl

   < 0.5

   FeSO4

   33.4 ± 0.5

   0.1 M

   126.0 ± 3.2

   NaCl

   < 0.5

   Pb(Ac)2

   26.9 ± 0.4

   0.2 M

   148.8 ± 4.1

   FeCl3

   < 0.5

   AgNO3

   8.2 ± 0.4

   0.5 M

   349.4 ± 26.1

Anionc (1 mM)

Anionc (10 mM)

   1.0 M

   1346.5 ± 38.2

   Noneb

   100.0 ± 4.5

   Noneb

   100.0 ± 1.4

   1.5 M

   1501.5 ± 74.6

   CH3COO-

   108.4 ± 7.8

   SO42-

   110.4 ± 0.9

   2.0 M

   1333.5 ± 95.4

   NO3-

   102.6 ± 2.6

   SO32-

   109.1 ± 1.0

   2.5 M

   37.2 ± 7.5

   SO42-

   99.3 ± 3.4

   CH3COO-

   108.4 ± 2.2

   3.0 M

   114.3 ± 1.6

   Cl -

   97.4 ± 5.4

   Cl -

   104.5 ± 0.8

   3.5 M

   164.4 ± 8.1

   SO32-

   96.9 ± 3.5

   NO3-

   102.2 ± 2.7

   4.0 M

   170.9 ± 1.7

   PO43-

   93.2 ± 6.2

   PO43-

   68.0 ± 1.4

Modifying reagent (1 mM)

Detergent (0.1%)

Detergent (1%)

   Noneb

   100.0 ± 0.6

   Noneb

   100.0 ± 3.7

   Noneb

   100.0 ± 1.2

   PMSF

   13.1 ± 1.2

   CTAB

   175.0 ± 3.7

   Triton X-100

   34.3 ± 0.3

   DEPC

   35.4 ± 0.4

   NLS

   130.5 ± 0.1

   NP40

   29.0 ± 0.5

Chelating agent (10 mM)

   Triton X-100

   114.1 ± 3.6

   NLS

   16.9 ± 0.4

   Noneb

   100.0 ± 1.5

   NP40

   102.8 ± 2.6

   Tween 40

   15.4 ± 0.7

   EDTA

   50.0 ± 2.4

   Tween 20

   56.4 ± 1.8

   Tween 20

   15.4 ± 0.2

   EGTA

   22.4 ± 0.6

   SDS

   50.7 ± 2.4

   Tween 80

   12.9 ± 0.3

Emulsifying agent

   Tween 40

   38.6 ± 1.0

   CTAB

   12.0 ± 0.7

   Noneb

   100.0 ± 2.2

   Tween 80

   32.6 ± 0.3

   SDS

   8.8 ± 0.2

   Gum arabic (0.5%)

   186.5 ± 1.3

  1. All measurements were performed using the p NPP method. Standard errors of the mean values are shown. a The enzyme was preincubated with 1 mM EDTA in order to chelate any metal bound to the enzyme molecule prior to cation addition. b Reference compound/condition set as 100% activity. c All anions from sodium salts to avoid cation interference. d The specific activity for this compound was 196.5 U/mg. e Apparent optimum temperature over 1 h reaction time.