Lipase (MS), CAS No.9001-62-1

CAS: 9001-62-1 Cat. No.: L1523262 Numéro CE: 232-619-9 PubChem CID: 135534490

GRADE & PURITY Suitable for mass spectrometry (MS), Native, EnzymoPure™, ≥99%(HPLC), from Porcine Pancreas, ≥20000 U/mg protein

Vue d’ensemble

Lipase catalyzes the hydrolysis of triacylglycerols in aqueous solution to produce glycerol and free fatty acids. This lipase is derived from porcine pancreas. In PBS buffer or Tris‑HCl buffer: Triglyceride + H₂O → Diglyceride + Fatty Acid Dissolution Solution Lipase is dissolved in 100 μL of 5 mM calcium chloride (ice bath before use). pH Range Lipase exhibits optimal activity at pH 7.7. Application This lipase specifically hydrolyzes triacylglycerols in serum or animal tissue samples. Enzymatic Hydrolysis SOP (For Reference Only) Dilute 20 μL serum sample with 20 μL of 100 mM PBS buffer to pH 7.7, incubate at 37 °C for 30 min, immediately add 2–6 μL lipase, and incubate for 15 min.

Specifications

Product Name

Lipase (MS), CAS No.9001-62-1

Grade

Native, Suitable for mass spectrometry (MS), EnzymoPure™

Spécifications et pureté

EnzymoPure™,suitable for mass spectrometry (MS),Native,≥99%(HPLC),from Porcine Pancreas, ≥20000 U/mg protein

CAS

9001-62-1

Numéro de commission de l'enzyme

EC 3.1.1.3

Type de molécule

Enzyme

Product Line

Produits biologiques

Stockage et expédition

Concentration

from Porcine Pancreas, ≥20000 U/mg protein

Conditions de stockage de stockage

Store at -20°C

Expédié en

Ice chest + Ice pads

Définition de l'unité

The amount of enzyme required to hydrolyze triglyceride to release 1.0 microequivalents of fatty acids in 1 hour with olive oil as a substrate at pH 7.7 and at 37°C.

Application Protocols

Not specified for this item; refer to CoA/Spec Sheet.

Note: For general literature procedures (e.g., lipase-catalyzed hydrolysis or transesterification, or MS sample prep), consult peer-reviewed protocols and adapt conditions to the specific source and formulation of this lipase.

Biological Roles

• Function (general biology)

  • Lipases are serine hydrolases that hydrolyze ester bonds of triacylglycerols to release free fatty acids and glycerol, playing central roles in lipid digestion, transport, and cellular lipid homeostasis.

• Mechanism and structure (literature)

  • Utilize a catalytic Ser–His–Asp triad and often exhibit interfacial activation upon binding to lipid droplets/micelles. Many possess a lid domain that modulates access to the active site.

• Distribution

  • Found across taxa (bacteria, fungi, plants, animals). Specific source and isoform for this item are not specified; refer to CoA/Spec Sheet.

• Biochemical pathways

  • Involved in triglyceride turnover, β-oxidation priming (by generating fatty acids), and remodeling of lipid assemblies. In microbes, lipases contribute to nutrient acquisition and biofilm dynamics.

• Note

  • This product is intended strictly for research and laboratory use; no clinical or diagnostic claims are made.

Buffer Applications

This enzyme is not itself a buffering reagent; however, successful use depends on appropriate buffer systems.

• Common buffer systems for lipase work (literature/general)

  • Phosphate buffer: 10–100 mM, pH 6.8–7.4, robust buffering but non-volatile (less suitable for direct MS injection).
  • Tris buffer: 10–100 mM, pH 7.5–8.5, good for many lipases; partially manageable for MS after desalting/lyophilization.
  • HEPES: 10–50 mM, pH 7.2–8.0, excellent biological buffer; non-volatile for MS.
  • Ammonium bicarbonate/acetate: 25–100 mM, pH ~7.5, volatile—preferred for MS sample prep to minimize non-volatile residues.

• Additives (as needed; literature)

  • Salts: 50–150 mM NaCl can aid solubility/stability; verify MS compatibility.
  • Ca2+: Some lipases are stabilized/activated by calcium—avoid strong chelators (e.g., EDTA) if Ca2+ dependence is suspected for your enzyme source.
  • Glycerol: 5–20% v/v may improve storage stability but is non-volatile; remove prior to MS.

• Practical tips

  • Filter-sterilize buffers (0.22 µm) to minimize microbial protease contamination.
  • For MS workflows, keep buffer ionic strength minimal and use volatile components; plan a cleanup step (e.g., SPE, spin filters) if non-volatile additives are unavoidable.

Green Alternatives

Enzymatic catalysis by lipases is frequently a greener alternative to traditional chemical ester manipulations.

• Comparative view (general/literature)

  • Lipase-catalyzed esterification/transesterification vs acid/base catalysis:
    • Conditions: Ambient temperature, atmospheric pressure, near-neutral pH vs strong acids/bases and elevated temperatures.
    • Selectivity: High chemo-, regio-, and enantioselectivity vs lower selectivity and protection/deprotection overhead.
    • Waste: Aqueous buffers and benign co-solvents vs corrosive mineral acids/bases and salt waste.
    • Energy: Lower energy input due to mild conditions.

• Small comparison table (general)

  • Lipase route: Mild, selective, reusable (especially when immobilized); compatible with green solvents (e.g., 2-MeTHF, CPME, EtOAc) under low water activity. Tradeoffs: Possible enzyme cost, sensitivity to solvents, need for water activity control.
  • Conventional route: Mineral-acid or base catalysis in petrochemical solvents; robust to impurities, lower catalyst cost. Tradeoffs: Racemic products, harsher conditions, more neutralization waste.

• MS workflow advantages

  • MS-suitable enzyme preparations reduce the need for extensive desalting/cleanup (less solvent consumption and instrument fouling), though verification against CoA is recommended for this specific lot.

Pharmaceutical Uses

This product is supplied for research use only; no therapeutic or clinical applications are claimed.

• Formulation/manufacturing context (general/industry practice)

  • Processing aid in biocatalytic steps for ester formation/cleavage during small-molecule intermediate synthesis, where enzymatic selectivity can reduce protecting-group manipulations.
  • Analytical reagent for quality control of lipid-containing formulations (e.g., enzymatic hydrolysis to profile fatty acid composition by LC–MS/GC–MS).

• Standards and compendia

  • No pharmacopeial status is claimed for this specific item. Any use in GMP contexts requires independent qualification and review of lot-specific CoA/SDS.

• Important note

  • Specifications such as endotoxin, bioburden, host-cell proteins, and residual solvents/excipients are not specified for this item; refer to CoA/Spec Sheet if required for regulated workflows.

Physical Properties

Proteins/enzymes do not have conventional small-molecule constants like BP/MP. Relevant handling properties are solution behavior and stability.

• Item-specific physical data

  • Appearance: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.

• Solubility and solution behavior (general/literature)

  • Solubility: Typically soluble in aqueous buffers (e.g., 10–100 mM Tris, HEPES, or phosphate, pH 7–8); solubility and stability can depend strongly on ionic strength and additives.
  • Organic co-solvents: Low percentages (≤10–20% v/v) of water-miscible solvents (e.g., glycerol, ethanol, isopropanol, DMSO) may be tolerated by some lipases; activity often decreases with increasing organic content unless immobilized or engineered.
  • pH activity window: Many lipases show activity from pH ~6–9 (literature; enzyme/source-dependent).
  • Temperature activity window: Typical operational range 20–40°C; thermal stability is source-dependent (literature).

• Other constants (literature/general)

  • pKa, logP, refractive index, BP/MP: Not applicable to proteins.
  • Isoelectric point (pI): Varies by source/sequence; consult CoA for the supplied preparation if specified.

Quality and Grades

• Item-specific grade information (from Product Data)

  • Suitable for mass spectrometry (MS): Indicates the preparation is optimized to minimize non-volatile salts, detergents, and adduct-forming contaminants that can suppress ionization or contaminate MS instrumentation. Practical benefit: cleaner spectra and reduced background in proteomics or enzymology–MS workflows.
  • Native: The enzyme is provided in a non-denatured form suitable for activity-dependent applications, assuming appropriate buffer and temperature conditions.
  • EnzymoPure™: Branded indication of high purity suitable for enzymology. Exact specifications (e.g., specific activity, residual nucleases/proteases, host-cell proteins) are not specified for this item; refer to CoA/Spec Sheet.

• What this means in practice (general guidance)

  • MS-suitable enzyme preparations typically avoid glycerol at high percentages, non-volatile buffers (e.g., high phosphate), and surfactants that compromise ESI/MALDI; or they use volatile salts (e.g., ammonium acetate) to facilitate cleanup. Verify with CoA.
  • Native status supports biocatalysis, kinetic resolution, and hydrolytic/transesterification assays. Handle gently to maintain tertiary structure.

• Not specified for this item; refer to CoA/Spec Sheet

  • Source organism, specific activity (U/mg), purity (%), excipients/stabilizers, residual moisture, and endotoxin/bioburden.

Reaction and Applications

• Catalytic function (general)

  • Lipases (EC 3.1.1.3) catalyze hydrolysis of triacylglycerol ester bonds at the lipid–water interface. In low-water or organic media, the equilibrium shifts to esterification and transesterification, enabling synthetic transformations.

• Research and analytical uses (general; expandable from MS-grade context)

  • Sample preparation for lipid analysis: Selective hydrolysis of triglycerides or phospholipids prior to LC–MS/MS, aiding structural elucidation or quantitation by simplifying lipid mixtures.
  • Enzymatic derivatization: Formation or cleavage of esters for improved chromatographic/MS behavior (e.g., generating free fatty acids for derivatization).

• Synthetic/biocatalytic applications (literature)

  • Kinetic resolution of secondary alcohols or chiral esters via selective acylation/deacylation.
  • Transesterification for biodiesel-related model reactions and fine chemical synthesis.
  • Regioselective protection/deprotection steps in carbohydrate and nucleoside chemistry using vinyl or isopropenyl esters as acyl donors.

• Practical tips (literature)

  • pH: Many lipases prefer neutral to slightly basic conditions (pH 7–9). Use appropriate buffers; check source-specific optima.
  • Temperature: 20–40°C commonly balances rate and stability; avoid prolonged exposure above the enzyme’s Tm.
  • Cofactors: Not generally required; some lipases are stabilized by Ca2+ (avoid chelators if Ca2+ dependence is known for the source).
  • Interfacial activation: Incorporate emulsifiers or substrate emulsions to maximize hydrolysis; avoid denaturing surfactants if activity is needed.

For item-specific activity units, source, or formulation, see the CoA/Spec Sheet (not specified here).

Reaction Conditions

Typical conditions vary with substrate and lipase source; the following are general literature guidelines.

• Hydrolysis (aqueous)

  • Buffer: 50 mM phosphate or Tris, pH 7.0–8.0.
  • Temperature: 25–37°C.
  • Substrate delivery: Emulsify triglycerides with gentle surfactants (e.g., gum arabic, bile salt mimetics) or mechanical stirring; avoid denaturing surfactants (SDS).
  • Time: 0.5–24 h depending on load and emulsification.

• Transesterification/esterification (low-water/organic)

  • Solvent: MTBE, tert-amyl alcohol, heptane, 2-MeTHF, or EtOAc; water activity controlled via molecular sieves or salt hydrates.
  • Acyl donors: Vinyl acetate/propionate, isopropenyl acetate, acid anhydrides.
  • Temperature: 25–50°C (higher temps risk denaturation for non-immobilized enzymes).
  • Enzyme format: Immobilized enzymes are preferred for organic media; native soluble enzymes may lose activity (check compatibility).

• MS-focused sample prep (general)

  • Buffer: 25–50 mM ammonium bicarbonate, pH ~7.8, at 30–37°C.
  • Cleanup: Desalt via C18/SPE or spin filters before direct infusion/LC–MS.

• Expected outcomes (literature)

  • Enantiomeric excess in kinetic resolutions can exceed 90% for suitable substrates; conversions range from 50–99% depending on equilibrium and water activity. These values are substrate- and enzyme-dependent.

Item-specific activity units, loading, and source are not specified; consult CoA/Spec Sheet.

Safety and Handling

• GHS classification and hazard statements

  • Signal word: Not specified for this item; refer to SDS.
  • H-statements: Not specified for this item; refer to SDS.
  • Pictograms: Not specified for this item; refer to SDS.

• General safety guidance for enzymes/proteins (literature/best practice)

  • Potential allergenicity: Enzymes can act as respiratory/skin sensitizers. Avoid generating aerosols and dust from dry/lyophilized material.
  • PPE: Use laboratory coat, gloves (nitrile), and safety glasses. Handle in a fume hood or biosafety cabinet when weighing powders to minimize inhalation risk.
  • First aid (overview; defer to SDS): If inhaled—move to fresh air; if on skin—wash with soap and water; if in eyes—rinse cautiously with water; if ingested—rinse mouth and seek medical advice.
  • Incompatibilities: Strong oxidizers and extremes of pH/temperature can denature proteins. Avoid proteases and microbial contamination.
  • Spill response: Avoid dust; gently cover with damp absorbent material, collect, and dispose per institutional and local regulations.

• Storage and stability

  • Store at −20°C (per Product Data). Keep tightly closed, desiccated, and protected from repeated freeze–thaw. For working solutions, maintain on ice and aliquot to avoid activity loss.

Always consult the product-specific SDS for authoritative hazard and response information.

Solvent Selection

For protein enzymes, “solvent selection” centers on buffer composition and, where relevant, controlled use of co-solvents.

• Polarity/matrix

  • Aqueous buffers are preferred to maintain native structure and activity. Typical choices: Tris, HEPES, or phosphate buffers (10–100 mM), pH tailored to the lipase source (often pH 7–8; literature).

• Co-solvent tolerance (literature/general)

  • Low levels of water-miscible organic solvents (≤10–20% v/v ethanol, isopropanol, acetone, DMSO, glycerol) may be tolerated with variable effects on activity/stability. Immobilized lipases often show higher tolerance and can function in nearly anhydrous organic solvents for transesterification.

• When to choose alternatives

  • For MS workflows, prefer volatile buffers (e.g., ammonium bicarbonate/acetate) to reduce salt adducts. Avoid non-volatile detergents (e.g., SDS) unless absolutely required and removed prior to MS.
  • For preparative biocatalysis in organic media, consider immobilized lipase formats to enhance stability and reuse; this listing is a native enzyme (format/excipients not specified—see CoA).

• Simple comparison (general)

  • Tris vs phosphate: Tris offers good buffering near pH 8 and is volatile enough for some MS prep after lyophilization; phosphate buffers strongly at pH ~7.2 but are non-volatile and MS-unfriendly.
  • HEPES: Excellent biological buffer (pKa ~7.5) but non-volatile; avoid in direct-injection MS samples.

Storage and Reconstitution

• Item-specific storage and shipping (from Product Data)

  • Storage: Store at −20°C.
  • Shipped: In an ice chest with ice pads to maintain a cold chain.

• Stability notes (general best practice)

  • Avoid repeated freeze–thaw cycles; aliquot upon first receipt. Keep working solutions on ice and use within the same day where possible.
  • Protect from microbial contamination; use sterile buffers and tools.

• Reconstitution (not specified for this item)

  • Reconstitution solvent, concentration, excipients, and activity units are not specified for this item; refer to CoA/Spec Sheet.
  • General guidance (literature): If supplied as a lyophilized powder, reconstitute gently in chilled buffer suitable for your application (e.g., 10–50 mM Tris or ammonium bicarbonate, pH ~7.5–8.0). For MS workflows, prefer volatile buffers and minimize non-volatile additives; perform desalting prior to analysis.

• Storage after reconstitution (general)

  • Short term (hours–days): 2–8°C.
  • Longer term: −20°C or below in aliquots; consider addition of stabilizers such as 10–20% glycerol only if compatible with downstream use (remove prior to MS).

Structure and Identity

Lipase (MS) is a protein enzyme (triacylglycerol acylhydrolase; EC 3.1.1.3) supplied in a grade suitable for mass spectrometry workflows.

• Item-specific identifiers (from Product Data)

  • SKU: L1523262
  • Product name: Lipase (MS)
  • CAS: 9001-62-1
  • Grade/Purity: Suitable for mass spectrometry (MS), Native, EnzymoPure™
  • Storage: Store at −20°C
  • Shipped: Ice chest + ice pads
  • Research use: For research use only
  • Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
  • InChIKey: Not applicable to heterogeneous protein materials.
  • SMILES: Not applicable to proteins/enzymes.

• Structural features (general/protein literature)

  • Enzyme class: Serine hydrolase; typical catalytic triad Ser–His–Asp/Glu located within an α/β-hydrolase fold.
  • Substrate scope: Triacylglycerols and related esters; many lipases show interfacial activation via a movable lid domain.
  • Quaternary/heterogeneity: Commercial lipase preparations can be mixtures of isoforms/glycoforms depending on the biological source (not specified for this item; refer to CoA/Spec Sheet).

• 2D description in words (general)

  • Polypeptide chain(s) composed of L-amino acids forming an α/β core; active-site serine in a nucleophilic elbow; hydrophobic surface patches support binding to lipid–water interfaces.

Synthetic Utility

Lipase catalysis is widely leveraged for selective ester transformations under mild conditions.

• Key reactivities (literature)

  • Hydrolysis of esters: Preferential cleavage of one acyl group in polyesters or triglycerides; regioselectivity can be tuned by substrate and conditions.
  • Transesterification/esterification: Using vinyl or isopropenyl esters as acyl donors drives reactions irreversibly by acetaldehyde/ketone removal.
  • Kinetic resolution: Resolution of racemic secondary alcohols or acids via differential acylation/deacylation (E values often >50 for favorable substrates).

• Retrosynthetic value

  • Introduces chirality or enriches enantiomers without chiral auxiliaries. Facilitates protecting-group strategies via chemoselective manipulation of one ester site in multifunctional molecules.

• Compatibility and media

  • Aqueous emulsions for hydrolysis; low-water organic solvents (e.g., MTBE, toluene, heptane, 2-MeTHF, EtOAc) for synthesis—often with immobilized enzymes to enhance activity and recyclability (general guidance; verify suitability for a native preparation).

• Workup advantages

  • Mild conditions simplify downstream purification; enzymes can be removed by filtration (if immobilized) or precipitation/ultrafiltration.

Target Specificity

Not applicable. This product is an enzyme reagent (lipase), not an affinity reagent or antibody. No target/epitope specificity, isotype, clone, or species reactivity is provided for this item.