| HS Code | 807898 |
| Enzyme Type | protease |
| Source | Saccharomyces cerevisiae |
| Physical Form | powder |
| Solubility | soluble in water |
| Optimum Ph | 5.0-7.0 |
| Optimum Temperature | 45-55°C |
| Activity Concentration | 500,000 U/g |
| Storage Stability | stable for 12 months at 4°C |
| Inactivation Conditions | inactivated above 70°C |
| Applications | protein hydrolysis and peptide production |
As an accredited Yeast Proteolytic Enzyme factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | 500 g sealed HDPE bottle with desiccant, child-resistant cap, and hazard label for safe enzyme storage. |
| Container Loading (20′ FCL) | 20′ FCL: Yeast Proteolytic Enzyme in sealed drums/bags, palletized, dry, non-hazardous, loaded tight to prevent shifting. |
| Shipping | Ship yeast proteolytic enzyme in sealed, moisture-resistant containers under temperature-controlled conditions, ideally refrigerated (2–8°C) if liquid. Use insulated packaging with ice packs, avoid freezing, and protect from heat and humidity. Label as biological/enzyme material. Ensure compliant documentation and prompt delivery to preserve activity and stability. |
| Storage | Store Yeast Proteolytic Enzyme in a tightly sealed, moisture-proof container at 2–8°C. Protect from light, humidity, and heat exposure. Keep away from oxidizing agents and strong acids/bases. Use clean, dry spatulas to prevent contamination. Do not freeze unless specified. Follow manufacturer’s label for expiration and handling. |
| Shelf Life | Shelf life is typically 12 months when stored airtight at 2–8°C, protected from moisture, heat, and direct light. |
During continuous production of hydrolysed vegetable protein seasoning bases, the yeast-derived proteolytic enzyme is metered into an aqueous suspension of defatted soy or pea protein concentrate adjusted to 8–12% w/w protein. The dosage window on a protein dry matter basis is 0.1–0.8% w/w; the lower boundary is applied when extended residence times above 8 h are available and the upper boundary reserved for reactor cycles constrained to 4 h. Hydrolysis is conducted in a jacketed CSTR with a retreat-curve impeller at 45–55°C; pH is maintained at pH 5.8–6.8 by 1.0 M NaOH dosing under pH-stat control. The pH-stat signal is converted to degree of hydrolysis using the standard NaOH consumption equation; an abrupt plateau below target is treated as phytate-induced cation chelation in soy substrate lots, corrected by adding food-grade calcium chloride at 0.02% w/w slurry before any re-dosing. The reaction is terminated in a plate-and-frame heat exchanger at 85°C for 10 min; residual water is then removed by a falling-film evaporator to 40–50% solids and the liquor is spray dried using nozzle atomization at inlet 180–200°C and outlet 85–95°C. Terminal product types include hydrolysed vegetable protein powder, liquid seasoning bases, and paste bouillon concentrates. Compliance is governed by Regulation (EC) No 1332/2008 for food enzymes, with manufacturing hygiene audited under ISO 22000:2018; in jurisdictions outside the EU, FCC monograph identity for protease activity and heavy-metal limits below the monograph threshold are applied to each batch certificate.
Commercially, the enzyme is dissolved in the brine phase at 0.02–0.3% w/w of raw meat block, either through low-pressure multi-needle injection or during vacuum tumbling. Phosphate in the same brine raises pH to 6.2–7.0; the preparation is not combined with acidified marinades below pH 5.0, because activity loss under such conditions makes batch control unreliable. When a 2–4°C meat mass is tumbled under 0.85–0.95 bar vacuum for 45–90 min, frictional heat rise remains below 6°C, keeping the enzyme within its working range. Subsequent holding at 4°C for 6–24 h allows controlled cleavage of myofibrillar proteins without extensive surface softening; if extended beyond 30 h, the outer 5–10 mm of the muscle block shows excessive texture loss. Terminal products include marinated whole-muscle turkey, shoulder bacon slabs, and restructured cooked hams. Compliance for US market use requires listing in USDA Food Safety and Inspection Service Directive 7120.1 as a safe and suitable ingredient for meat and poultry; EU establishments audit the same use as a processing aid under Regulation (EC) No 1332/2008 and the hygiene requirements of Regulation (EC) No 852/2004.
Rendered poultry viscera and whole fish frames are ground to 2–5 mm particle size and combined with water to a slurry at 12–18% protein before the enzyme is dosed at 0.05–0.25% w/w of raw slurry protein. The reactor is held at 50°C and pH 6.5–7.5 for 2–6 h; pH is corrected with 1.0 M potassium hydroxide to avoid excess sodium in the final pet food digests. Soluble protein is monitored by Kjeldahl after trichloroacetic acid precipitation; hydrolysis is stopped when the lot-specific release threshold is reached. The hydrolysate is then heat-inactivated at 90°C for 15 min, centrifuged to reduce bone fragments, and concentrated to 50% solids. The liquid palatant is either pumped to a vacuum coater for post-extrusion application at 0.5–2.0% by weight of kibble or spray dried onto maltodextrin carriers. Terminal product types include liquid cat food palatability enhancers, dry poultry liver digest powder, and canine kibble coating slurries. In the EU, the enzyme preparation is assessed under Regulation (EC) No 1831/2003; in North America, AAFCO Official Publication ingredient definitions and GRAS enzyme preparation records govern label acceptance.
In cosmetic peptide manufacture, collagen, keratin, or silk fibroin is suspended to 5–10% w/w protein in deionized water and adjusted to pH 6.5–7.5; the enzyme is added at 0.5–1.5% w/w of dry protein. The reaction is carried out at 40–50°C for 4–8 h in a recirculating membrane reactor fitted with a 10 kDa ultrafiltration cassette; crossflow velocity is controlled to maintain transmembrane pressure below 1.0 bar so that gel-layer fouling does not sharply reduce flux in the second half of the run. The permeate is passed through a 3 kDa membrane to select the 1–3 kDa peptide fraction; retentates above 10 kDa are recycled to the reactor for further hydrolysis. The final fraction is sterile-filtered through 0.22 µm polyethersulfone cartridges, concentrated by reverse osmosis, and lyophilized to ≤5% moisture. Terminal products include hydrolysed collagen powder for skin conditioning, silk peptide solutions for hair care emulsions, and low-molecular-weight peptide complexes for scalp treatments. Production hygiene and batch traceability comply with ISO 22716:2007; the finished cosmetic ingredient must satisfy safety assessment data requirements of Regulation (EC) No 1223/2009, Annex I, with residual enzyme activity declared only if the preparation is not removed by the membrane cascade.
Once unhydrolyzed soy globulins precipitate at their isoelectric point after enzyme dosing, the process sequence for partially hydrolysed soy or pea protein must be rearranged to avoid spray-dryer feed blockage. The enzyme is added at 0.2–1.0% w/w of protein to a 10% w/w isolate dispersion maintained at pH 7.0–7.5 with 1.0 M sodium hydroxide. Reaction proceeds at 50°C for 3–8 h; release criteria are set by 12% trichloroacetic acid solubility and osmolality. After inactivation at 90°C for 15 min, the liquor is adjusted to pH 3.8–4.2 to flocculate unhydrolyzed globulin aggregates, which are removed by disc-stack centrifugation. The clarified liquor is neutralized to pH 6.8, pasteurized, concentrated, and spray dried. Terminal materials include partially hydrolysed soy peptide isolate, pea protein hydrolysate powder, and cold-soluble protein fractions for ready-to-mix functional beverages. Compliance declarations are tied to ISO 9001:2015 and food safety prerequisite programmes under ISO 22000:2018; any destination market for low-allergen claims requires additional clinical substantiation beyond the enzyme supplier's standard dossier. Published data for residual antigenic epitope reduction at this specific dosage window is limited, so safety assessment is performed lot-wise using an immunoassay method rather than inferred from degree of hydrolysis alone.
Accelerated fish sauce production uses the enzyme during an initial warm extraction stage rather than relying solely on endogenous viscera proteases. Salted anchovy or sardine molange at 12–18% NaCl is adverse to the enzyme, so the preparation is added at 0.1–0.5% w/w of fish protein before salt exceeds 5%. The low-salt hydrolysis stage is held at 45°C and pH 6.0–7.0 for 6–12 h under slow agitation in open-top or closed stainless steel vessels; dissolved protein and total nitrogen are measured before salt is incrementally added to reach 20–25% w/w. The mass is then transferred to ambient fermentation tanks for 2–6 months. Terminal product types include first-press clear fish sauce, fermented anchovy paste, and liquid seasoning bases derived from the early hydrolysate fraction. Compliance follows Codex STAN 302-2011 where applicable, with processing records maintained under ISO 22000:2018; EU importers may request supplementary histamine and volatile basic nitrogen audit data generated before the first commercial batch release.
Competitive Yeast Proteolytic Enzyme prices that fit your budget—flexible terms and customized quotes for every order.
For samples, pricing, or more information, please contact us at +8615365186327 or mail to admin@ascent-chem.com.
We will respond to you as soon as possible.
Tel: +8615365186327
Email: admin@ascent-chem.com
Flexible payment, competitive price, premium service - Inquire now!
YPE-1000 L is a concentrated liquid yeast proteolytic enzyme preparation derived from Saccharomyces cerevisiae, standardized to a declared minimum activity of 1000 protease units per gram against Hammarsten casein at pH 6.0 and 37 °C. The preparation contains a native mixture of endopeptidases and exopeptidases, including serine and aspartyl protease fractions, which hydrolyse intact proteins to lower-molecular-weight peptides and free amino acids. A companion grade, YPE-500 P, is supplied as a spray-dried powder for dry blending applications where liquid dosing is not practical. Both grades are intended for food-grade protein hydrolysis, meat tenderization, flavour development, and protein hydrolysate manufacture. The liquid product has a specific gravity of 1.05–1.10 g/mL, a shelf life of 12 months at 4–8 °C in sealed containers, and should not be used in formulations requiring kosher or halal verification unless a lot-specific certificate is provided.
Conformance is established by activity assay, physicochemical data, and microbial limits. One protease unit is defined as the quantity of enzyme that liberates 1 µg of tyrosine per minute from Hammarsten casein at pH 6.0 and 37 °C using the Folin-Ciocalteu reagent. Activity is reported as protease units per gram because yeast protease does not correspond to a single purified enzyme, and the casein-based method captures the combined action of its proteinase complement. For liquid shipments in 1000 L totes, the coefficient of variation between top, middle, and bottom sample points is typically below 5.0% when the material is recirculated for 10 min before sampling. A lot is rejected if activity falls below the declared minimum, if the pH shifts outside the stated range, or if microbial enumeration exceeds the limits in the table below. Compliance with the Food Chemicals Codex general monograph for enzyme preparations and the JECFA General Specifications for Enzyme Preparations Used in Food Processing is required, including lead not exceeding 5 mg/kg, arsenic not exceeding 3 mg/kg, and absence of Salmonella in 25 g.
| Grade | Form | Declared activity | Dry matter / moisture | pH | Microbial specification |
|---|---|---|---|---|---|
| YPE-500 P | spray-dried powder | 500 PU/g minimum | moisture ≤ 5.0% | 5.5–6.5 in 10% solution | total aerobic plate count ≤ 50,000 CFU/g; coliforms ≤ 10 CFU/g; yeast and mould ≤ 100 CFU/g |
| YPE-1000 L | liquid concentrate | 1000 PU/g minimum | dry substance ≥ 20% | 4.8–5.8 as-is | total aerobic plate count ≤ 10,000 CFU/g; coliforms ≤ 10 CFU/g; yeast and mould ≤ 50 CFU/g |
| YPE-2000 H | liquid high concentrate | 2000 PU/g minimum | dry substance ≥ 25% | 4.8–5.8 as-is | Salmonella absent in 25 g; Escherichia coli absent in 25 g |
Viscosity of YPE-1000 L at 25 °C is typically below 10 mPa·s, permitting transfer with diaphragm or peristaltic pumps rather than high-shear centrifugal pumps. At pH 4.0–7.5, the liquid remains stable for 24 h without significant activity loss. Below pH 3.5 or above pH 8.0, activity loss accelerates and process hold times should be limited to 2 h unless lot-specific stability data indicate otherwise.
Thermal inactivation of yeast proteolytic enzyme in aqueous systems follows pseudo-first-order decay under typical processing conditions. Process validation is required to establish the residual activity curve for each product lot, but general process guidance indicates that holding at 70 °C for 10 min reduces residual protease activity below 5 PU/g in liquid hydrolysates. At 60 °C for 15 min, the aspartyl and serine fractions may not be fully inactivated, and residual activity should be assumed unless verified by assay. This heat-labile character is the principal difference from papain, which often requires the product core to reach 75 °C or above for reliable inactivation. In meat products, the relatively low thermal stability of yeast protease reduces the risk of post-cooking softening and surface breakdown during distribution. For hydrolysate manufacture, thermal inactivation should be performed before evaporation or spray drying to prevent continued cleavage in concentrated retentate. Published data for this specific configuration is limited, and lot-specific inactivation confirmation is recommended when a shelf-stable beverage or infant-grade hydrolysate is the final matrix.
In stirred-tank hydrolysis, the enzyme is dosed after the substrate is dispersed and pH adjusted. For soy, pea, or casein substrates, addition of 0.5–2.0% of enzyme protein by weight of substrate is typical, with hydrolysis at 45–55 °C and pH 5.5–6.5 for 2–6 h. The resulting degree of hydrolysis generally falls between 10% and 20%, producing soluble peptides with moderate bitterness. A jacketed stainless-steel vessel with pitched-blade agitation at 60–80 rpm is sufficient; high-shear rotor-stator mixing is not required and may damage the enzyme. After hydrolysis, inactivation at 70 °C for 10 min is followed by clarification, optionally membrane filtration, and spray drying.
Meat tenderization using YPE-1000 L is conducted at 0.05–0.10% of green meat weight. The enzyme is diluted into injection brine at 4–8 °C and applied by needle injection or vacuum tumbling at 6–10 rpm for 4–12 h. Brine salt levels of 1.5–2.0% w/w have minimal effect on activity, but sodium tripolyphosphate above 0.4% may reduce hydrolysis rate. Prolonged contact beyond 12 h at 8 °C can cause excessive surface hydrolysis, visible loss of muscle fibre integrity, and purge accumulation. In dairy protein modification, the enzyme is added to pre-denatured whey protein isolate solutions at 0.1–0.5% of protein. A pre-denaturation step at 90 °C for 5 min increases cleavage efficiency because native whey proteins are less accessible to yeast proteases. Hydrolysis at 45–50 °C for 2–4 h reduces viscosity and improves heat stability after spray drying, but the enzyme must be inactivated at 70 °C for 10 min before evaporation.
The selection of yeast proteolytic enzyme over plant or bacterial preparations is governed by pH operating window, downstream inactivation temperature, and final peptide profile. Compared with papain, the yeast enzyme shows more complete inactivation in products cooked to internal temperatures below 70 °C, which prevents continued proteolysis during cold storage. Compared with bromelain, the yeast enzyme does not introduce pineapple-derived flavour note or require allergen labelling associated with fruit protease. Compared with alkaline bacterial protease from Bacillus licheniformis, the yeast enzyme operates at acidic-to-neutral pH and produces fewer extremely short charged peptides at the same degree of hydrolysis, which can reduce perceived bitterness in soy and pea hydrolysates. Compared with fungal acid protease from Aspergillus niger, the yeast system contains exopeptidase activity that increases free amino nitrogen more rapidly in yeast extract and flavour precursor applications. The table below summarises the operating differences.
| Property | Yeast protease | Papain | Bromelain | Bacterial alkaline protease | Fungal acid protease |
|---|---|---|---|---|---|
| Source | Saccharomyces cerevisiae | Carica papaya latex | Ananas comosus stem | Bacillus licheniformis | Aspergillus niger |
| pH optimum | 5.5–6.5 | 6.0–8.0 | 6.0–8.0 | 8.0–10.5 | 3.0–5.0 |
| Temperature optimum | 40–55 °C | 50–70 °C | 50–70 °C | 55–70 °C | 45–55 °C |
| Inactivation threshold | substantially inactivated at 70 °C for 10 min | often requires 75 °C core temperature | often requires 75 °C core temperature | requires 80 °C for 10 min or alkaline pH shift | substantially inactivated at 65 °C for 15 min |
| Major inhibition | serine and aspartyl protease inhibitors | thiol-blocking agents, oxidants, heavy metals | thiol-blocking agents, oxidants, heavy metals | serine protease inhibitors, high-alkali instability | pepstatin, pH above 6.5 |
| Typical application | moderate DH hydrolysates, meat tenderization, yeast extract acceleration | high-temperature meat tenderization, difficult-to-inactivate processes | meat and seafood tenderization, juice fining | high-DH vegetable protein hydrolysates, alkaline cleaning compatibility | acidic protein hydrolysis, flavour development |
In rice and wheat protein hydrolysis, the lower pH optimum of yeast protease allows processing without a neutralization step after alkaline extraction, which reduces sodium load in the final hydrolysate. In contrast, alkaline bacterial protease requires pH adjustment to 8.0–10.5 and subsequent neutralization, producing salt and altering mineral profile. Processors switching from papain to YPE-1000 L should revalidate thermal process records because shorter residual activity in the finished matrix changes cold-chain tolerance and purge behaviour in meat products.
Oxidative sanitizers degrade yeast proteolytic enzyme activity by oxidising amino acid side chains and destabilising the protein fold. If peracetic acid or hydrogen peroxide is used for line sanitization, the line must be flushed with potable water until residual oxidizer is below 1 ppm before enzyme introduction. Residual peracetic acid at 5 ppm has been observed to reduce activity by more than 20% within 15 min at 25 °C in process waters of low organic load. The enzyme should not be mixed with sulfite, metabisulfite, or high concentrations of reducing sugars above 10% in solution for extended hold periods because Maillard-type interactions with enzyme amines reduce active-site availability. The liquid preparation is incompatible with strong acids below pH 2.5, strong bases above pH 9.0, and polar solvents above 10% v/v. In dry-blend operations, YPE-500 P should be added after hygroscopic ingredients are sealed in individual feeders to prevent moisture uptake. At ambient relative humidity above 60%, bulk powder exposure should be limited to 8 h to preserve flow and activity.
Pumps, load cells, and dosing skids in liquid enzyme lines should be constructed from 316L stainless steel or food-grade high-density polyethylene. Copper, iron, and aluminium surfaces should be avoided because leached metal ions accelerate protein denaturation and may exceed finished-product limits. In batch records, enzyme lot number, date of thawing, and residual sanitizer concentration should be logged because these factors explain most unexplained variation in hydrolysis rate. When process deviations fall outside the validated temperature, pH, or sanitizer residual limits, the batch is typically re-assayed for free amino nitrogen rather than released solely by final thermal processing because thermal inactivation does not reverse the formation of undesirable peptide off-notes.
For yeast extract acceleration, the enzyme is added to a 10–15% yeast slurry at 0.1–0.3% w/w and held at 50 °C for 12–24 h. The addition of yeast protease shortens autolysis time and increases free amino nitrogen, but the exact gain depends on strain, slurry solids, and nitrogen source. A final heat treatment at 85 °C for 15 min is applied to terminate enzyme action and pasteurise the extract. Published data for this specific configuration is limited; processors are advised to establish substrate-specific dose-response curves using the same yeast cream and salt profile intended for production.
