Lipase

<p>Lipase 15 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 25°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 15 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (13 %), laurate (1 %), palmitate (1 %), stearate (&lt;1 %), arachidate (&lt;1 %) and behenate (&lt;1 %).</p>

<p>Lipase 68 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-9 and temp. optimum at 30°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 68 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (75 %), laurate (8 %), palmitate (1 %) and stearate (0.1 %).</p>

<p>Lipase 64 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 64 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (0.5 %) and laurate (0.1 %).</p>

<p>Lipase 17 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 17 was shown to hydrolyze p-Nitrophenyl esters of butyrate (2 % activity compared to octanoate), octanoate (100 %), laurate (20 %), palmitate (3 %), stearate (1 %), arachidate (1 %) and behenate (1 %).</p>

<p>Lipase 14 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 30-40°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 14 was shown to hydrolyze p-Nitrophenyl esters of butyrate (74 % activity compared to octanoate), octanoate (100 %), laurate (8 %), palmitate (5 %), stearate (4 %), arachidate (1 %) and behenate (0.6 %).</p>

<p>Lipase 16 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at &gt;40°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 16 was shown to hydrolyze p-Nitrophenyl esters of butyrate (58 % activity compared to octanoate), octanoate (100 %), laurate (40 %), palmitate (27 %), stearate (13 %), arachidate (2 %) and behenate (0.2 %).</p>

<p>Lipase 01 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 25-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 01 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (57 %), laurate (13 %), palmitate (9 %), stearate (6 %), arachidate (2 %) and behenate (0.1 %).</p>

<p>Lipase 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).</p>

<p>Lipase 70 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 70 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (62 %), laurate (15 %), palmitate (4 %), stearate (3 %), arachidate (2 %) and behenate (0.2 %).</p>

<p>Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).</p>

<p>Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).</p>

<p>Lipase 30 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 5.5-8 and temp. optimum at &gt;55°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 30 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (72 %), laurate (38 %), palmitate (7 %) and stearate (2 %).</p>

<p>Lipase 13 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 13 was shown to hydrolyze p-Nitrophenyl esters of butyrate (87 % activity compared to octanoate), octanoate (100 %), palmitate (44 %), stearate (21 %) and arachidate (2 %).</p>

<p>Lipase 67 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 67 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (37 %), laurate (3 %) and palmitate (0.2 %).</p>

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.</p>

<p>Lipase 12 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7.5 and temp. optimum at &gt;60°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 12 was shown to hydrolyze p-Nitrophenyl esters of butyrate (60 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (30 %), stearate (14 %), arachidate (0.2 %) and behenate (0.2 %).</p>

<p>Lipase 08 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 20-60°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 08 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (60 %), laurate (7 %), palmitate (0.5 %), stearate (0.2 %), arachidate (0.1 %) and behenate (0.1 %).</p>

<p>Lipase 20 recombinantly expressed in P. pastoris comes in a spray-dried formulation. It has its pH optimum at 7-8. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 20 was shown to hydrolyze p-Nitrophenyl esters of butyrate (3 % activity compared to octanoate), octanoate (100 %), laurate (85 %), palmitate (52 %), stearate (29 %), arachidate (22 %) and behenate (8 %).</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).</p>