Sigma-Aldrich Bromelain from pineapple stem ≥4 units/mg protein, (chromatography purified)

Bromelain, derived from pineapple stem, is a cysteine endopeptidase enzyme with broad specificity for protein cleavage. It is widely used in biological research, food processing, and pharmaceutical applications for its proteolytic activity. This product is chromatographically purified to ensure high specificity and activity.

Product Properties:

Applications:

1. Biological Research:
   • Used as a positive control in SDS-PAGE zymograms for enzyme activity assays.
   • For assaying proteolytic activity using Azocasein substrate.
2. Pharmaceutical Applications:
   • Studied for its role in inhibiting proinflammatory prostaglandins biosynthesis.
   • Investigated for its potential to reduce clotting efficiency and as an anti-inflammatory agent.
3. Food Processing:
   • Used for enzymatic hydrolysis of honeybee-collected pollen to enhance digestibility.
4. Analytical Chemistry:
   • Employs pGlu-Phe-Leu-p-nitroanilide as a chromogenic substrate for precise activity assays.

Biochemical and Physiological Actions:

• Proteolytic Activity:
  Bromelain exhibits broad specificity for protein cleavage, facilitating various research applications.
• Cysteine Endopeptidase:
  Hydrolyzes proteins efficiently by targeting specific peptide bonds, useful in enzymatic reactions and therapeutic studies.

Unit Definition:

One unit of bromelain activity is defined as the amount of enzyme required to release 1.0 µmole of p-nitrophenol from N-α-Z-L-lysine p-nitrophenyl ester per minute at pH 4.6 and 25°C.

Preparation and Handling:

1. Reconstitution:
   • Dissolve in water at a concentration of 1 mg/mL to yield a clear, colorless solution.
2. Storage:
   • Store at −20°C to maintain enzyme activity and stability.

Advantages:

• High Purity:
  • Chromatographically purified for enhanced reliability and reproducibility.
• Wide Applicability:
  • Useful across proteomics, pharmaceuticals, and food science.
• Stable Formulation:
  • Lyophilized powder ensures long-term stability when stored as recommended.

References:

1. Study on SDS-PAGE zymograms and positive control use.
2. Azocasein substrate for proteolytic activity determination.
3. Enzymatic hydrolysates of honeybee pollen for enhanced bioavailability.

Sigma-Aldrich Bromelain from Pineapple Stem (≥4 units/mg protein) is a reliable and versatile enzyme ideal for proteolytic activity studies, pharmaceutical applications, and biological research. Its high purity, broad specificity, and stability make it an essential reagent for diverse enzymatic applications.