Products

ZA Biotech offers the following enzymes:

Lipase

Laccase

Nitrile Hydratase

Esterases

Chitinase

These enzymes are offered as free or immobilised products. ZA Biotech also offers other products eg. Kafirin 

The following enzymes are in R&D and will be available shortly:

Amidase

Nitrilase

Esterase (heat stable)

Lipoxygenase

Epoxide hydrolase

Subtilisin

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- Broad substrate range (Brady et al 2004).

-Yields of product on enzyme typically approach 100%, with >99% selectivity.

-Reactions occur at near neutral pH and ambient temperatures.

-We have recently demonstrated that in conjunction with an amidase this nitrile hydratase enzyme can   yield enantiomerically pure â-substituted carboxylic acids (Kinfe et al 2009).

-Currently produced by the wild type organism.  Heterologous expression system under development.

Biocatalysis: 

Enzymes are widely applied in the field of chemical organic synthesis.  Nitrile hydratase (EC 4.2.1.84) is an enzyme that converts nitrile groups to the corresponding amides by addition of a water molecule.

Activiry: Approximately 2000U/g  

Commercial Applications: 

A Rhodococcus rhodochrous nitrile hydratase activity is used to produce nicotinamide 3-cyanopyridine with ~100% yield, and a volumetric yield of 1465 g/L. It is also used to produce acrylamide (propeneamide).  

2.    LIPASE

The enzymatic activity determination is based on the de-esterification of tributyrin and 1 unit (U) corresponds to the amount of enzyme which liberates 1 µmol butyric acid per minute at pH 7.5 and 40°C. The assay is titrometric (pH Titrino, Metrohm) and measurers rate of sodium hydroxide (NaOH) addition to counteract the butyric acid formed during the reaction. The following solutions were prepared: Solution “A” was 25 mM potassium phosphate monobasic buffer pH adjusted with 1 M NaOH (pH 7.5), solution “B” was tributyrin (Acros organics) and solution “C” was the titrant (0.1 mM NaOH). The reactions were performed in a 30 ml jacketed vessel (40°C) connected to a temperature controlled water bath). Twenty millilitres of solution A was allowed to reach temperature followed by the dropwise addition of 1 ml of solution B. The reaction was initiated by the addition of 1 ml of lipase or lipase spherezymes at a concentration high enough to produce a readable rate. The initial rates of NaOH addition were used to determine lipase activities, which were measured in triplicate.