Bromelain for Gelatin Hydrolysis and Collagen Peptide Production
Produce functional food-grade collagen peptides and hydrolysed gelatin through controlled bromelain proteolysis at pH 5.0–8.0 and 45–65°C.
Collagen peptides and hydrolysed gelatin are among the fastest-growing functional food and nutraceutical ingredients globally, driven by consumer demand for joint health, skin elasticity, and sports nutrition products. The production of bioactive collagen peptides from animal-derived gelatin requires precise enzymatic hydrolysis to achieve target molecular weight distribution and functional characteristics — peptide chain length, amino acid composition, and solubility — that determine both the bioavailability and functional food properties of the finished ingredient. Gelatin, derived from the partial hydrolysis of collagen from bovine, porcine, or marine sources, is a high-molecular-weight protein (100,000–300,000 Da average, though this varies with processing) that forms gels at room temperature in aqueous solution. Full enzymatic hydrolysis to collagen peptides (typically 500–10,000 Da) produces a non-gelling, high-solubility protein ingredient that remains liquid at room temperature and can be spray-dried into a free-flowing powder with high protein content (90%+ on dry basis). Bromelain (EC 3.4.22.32) is widely used in collagen peptide production because its cysteine protease mechanism cleaves a different set of peptide bonds compared to the standard proteases used in initial gelatin hydrolysis (alcalase, pepsin, trypsin), providing distinct peptide profiles with specific bioactive sequence distributions. The combination of bromelain with other food-grade proteases in multi-enzyme hydrolysis systems is a commercial standard in premium collagen peptide production. Bromelain also demonstrates activity against native collagen (type I, II, III) in addition to denatured gelatin, making it useful in collagen extraction and preliminary hydrolysis steps where the triple-helical native structure is partially intact. In collagen peptide production, bromelain is typically applied at pH 5.5–7.5 and 50–60°C with dosage of 0.5–2.0% enzyme on gelatin protein weight, with reaction times of 1–6 hours depending on target DH (degree of hydrolysis) and molecular weight distribution. The reaction is stopped by heat inactivation at 85°C for 10–15 minutes, filtered for clarity, and the hydrolysate is spray-dried. Our food-grade bromelain is produced from Ananas comosus stem, standardised at 600–2,400 GDU/g, HALAL and KOSHER certified, with ISO 9001 and Food Grade documentation.
Bovine Collagen Peptide Production
Bovine gelatin (from hide or bone, typically pH 5.5–6.5, 8–12% solution at 55–60°C) is hydrolysed with bromelain at 1.0–2.0% on protein weight for 2–4 hours to achieve DH 15–25%, producing a collagen peptide distribution of 1,000–5,000 Da. The resulting hydrolysate has high solubility, no gelation at room temperature, and neutral flavour suitable for beverage and food fortification applications. Stop reaction at 85°C/10 min, filter, spray dry.
Marine Collagen Peptide from Fish Skin
Marine collagen from fish skin (typically Tilapia or Cod) has a lower denaturation temperature than bovine collagen and is suitable for enzymatic hydrolysis at 40–50°C. Bromelain at 0.5–1.5% on protein weight at pH 6.0–7.0 and 45–50°C for 2–3 hours achieves DH 20–30%, producing marine collagen peptides with high hydroxyproline content and a distinctive peptide mass profile. Marine collagen peptides are increasingly preferred in Asian beauty-food applications.
Multi-Enzyme Hydrolysis System — Bromelain + Alcalase
Sequential or simultaneous use of bromelain and alkaline protease (alcalase) provides complementary cleavage specificity, producing a broader peptide mass distribution and higher DH than either enzyme alone at equivalent loading. A typical protocol uses alcalase at pH 8.0 for initial hydrolysis, then bromelain at pH 6.0–7.0 for the secondary step after pH adjustment, achieving DH 30–40% in 4–6 hours total reaction time.
Functional Ingredient for Sports Nutrition
Collagen peptides produced with bromelain at DH 15–20% (MW 1,000–5,000 Da) meet the molecular weight specification for joint health and sports recovery products. High solubility at 10–15% concentration allows inclusion in clear beverage formats without turbidity. The amino acid profile (high glycine, proline, hydroxyproline) is maintained through controlled hydrolysis, and spray-dried collagen peptide powder has excellent flowability for high-speed capsule and sachet filling.
| Parameter | Value |
| Activity range | 600 – 2,400 GDU/g |
| Optimal pH | 5.0 – 8.0 |
| Optimal temperature | 45°C – 65°C |
| Form | Light yellow to tan powder |
| Shelf life | 24 months (sealed, cool, dry place) |
| Packaging | 25 kg drums / custom packaging |
Perguntas Frequentes
Why is bromelain used for collagen peptide production instead of other proteases?
Bromelain's cysteine protease mechanism provides different substrate cleavage specificity compared to serine proteases (trypsin, alcalase, pepsin) typically used in gelatin hydrolysis. This distinct specificity produces different peptide sequences and molecular weight profiles, including specific bioactive peptides such as GFOGER and KGHRGF-type sequences with potential joint health activity. In multi-enzyme systems, bromelain complements alcalase to provide broader coverage of peptide bond types, improving total DH and producing more functionally complete peptide profiles.
What is degree of hydrolysis (DH) and what level is target for collagen peptides?
Degree of hydrolysis (DH) measures the percentage of peptide bonds cleaved during enzymatic hydrolysis. For collagen peptides targeting joint health and skin applications, a DH of 15–25% typically produces a MW distribution of 1,000–5,000 Da suitable for GI absorption and systemic distribution. Higher DH (30–40%) produces smaller peptides below 1,000 Da with faster gastric transit and higher osmolality — more suitable for liquid sports nutrition formats. DH is measured by OPA (ortho-phthalaldehyde) method or Ninhydrin method and controlled by dose, time, temperature, and pH.
How do you stop the bromelain reaction to achieve a consistent peptide profile?
The bromelain hydrolysis reaction is stopped by heat inactivation: heating the hydrolysate to 85°C for 10–15 minutes denatures the enzyme irreversibly and stops further proteolysis. This is the standard termination method for food-grade enzyme reactions. pH adjustment to below 3.0 is an alternative but less preferred because it requires subsequent neutralisation. After heat inactivation, the hydrolysate is filtered for clarity and spray dried — the resulting peptide profile is stable and consistent across batches when temperature and time are controlled precisely.
What certifications are available for food-grade collagen peptide production?
Our bromelain for food applications carries ISO 9001, HALAL, KOSHER, and Food Grade certifications. We supply COA with GDU/g activity, protein content, moisture, heavy metals, microbial safety, and pH. For gelatin hydrolysis applications, we can provide source organism documentation (Ananas comosus stem), allergen statements (pineapple derivation), and country-of-origin documentation required for food ingredient regulatory compliance in EU (Novel Food), US (GRAS), and Asian markets.
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