SPRIN Protease Kit. Content Code Description Application. Covalently immobilised preparation of Subtilisin. Epoxy Acrylic Resin
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1 SPRIN Protease Kit SPRIN Protease Kit Normal (5 g each) Product code: SPKN SPRIN Protease Kit Large (20 g each) Product code: SPKL The kit contains four different covalently immobilised protease preparations, comprising Subtilisin and Thermolysin, on different polymeric carriers. Kit content: Content Code Description Application SPRIN epobond SUBTILISIN SBSME2 Covalently immobilised preparation of Subtilisin from Bacillus species on Epoxy Acrylic Resin Peptide synthesis/hydrolysis and peptide fragment condensation. Broad substrate specificity. SPRIN imibond SUBTILISIN SBSMH2 Covalently immobilised preparation of Subtilisin from Bacillus species on Amino Acrylic Resin Peptide synthesis/hydrolysis and peptide fragment condensation. Broad substrate specificity. SPRIN epobond THERMOLYSIN TGSME2 Covalently immobilised preparation of Thermolysin from Geobacillus species on Epoxy Acrylic Resin Peptide synthesis/hydrolysis of hydrophobic aminoacid containing peptides. Aspartame synthesis. SPRIN imibond THERMOLYSIN TGSMH2 Covalently immobilised preparation of Thermolysin from Geobacillus species on Amino Acrylic Resin Peptide synthesis/hydrolysis of hydrophobic aminoacid containing peptides. Aspartame synthesis. 1
2 Subtilisin is a protease characterized by a broad substrate specificity spectrum. It hydrolyzes peptide bonds preferably involving large uncharged residues, such as Phe, Tyr, Met, or Leu. When applied in water free system, the enzyme catalyzes the synthesis of peptides, displaying the same broad specificity. It also finds application in peptide fragments condensation. Thermolysin is a thermostable neutral metalloproteinase enzyme, requiring a zinc ion for enzyme activity. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. It preferentially cleaves -/-Phe or -/-Leu peptide bonds. It is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Geobacillus species. Description of each product: Product code: SBSME2 Specifications Covalently immobilised preparation of Subtilisin from Bacillus species Enzyme: Subtilisin Systematic name: Subtilisin, E.C Properties Activity: 2 U/g wet (casein assay, AM S044) Range ph of activity in buffer: , optimum 9.0 Range temperature: C, optimum 50 C Characteristics Matrix: epoxy acrylic polymer Particle size: μm Water content: 60 70% Product code: SBSMH2 Specifications Covalently immobilised preparation of Subtilisin from Bacillus species Enzyme: Subtilisin Systematic name: Subtilisin, E.C Properties Activity: 4.5 U/g wet (casein assay, AM S044) Range ph of activity in buffer: , optimum 9.0 Range temperature: C, optimum 50 C 2
3 Characteristics Matrix: amino acrylic polymer Particle size: μm Water content: 60 70% Product code: TGSME2 Specifications Covalently immobilised preparation of Thermolysin from Geobacillus species Enzyme: Neutral metalloproteinase Thermolysin Systematic name: Thermolysin, EC Properties Activity: 2 U/g wet (casein assay, AM S044) Range ph of activity in buffer: , optimum 8.0 Thermal stability below 70 C, optimum C Characteristics Matrix: epoxy acrylic polymer Particle size: μm Water content: 60 70% Product code: TGSMH2 Specifications Covalently immobilised preparation of Thermolysin from Geobacillus species Enzyme: Neutral metalloproteinase Thermolysin Systematic name: Thermolysin, EC Properties Activity: 2 U/g wet (casein assay, AM S044) Range ph of activity in buffer: , optimum 8.0 Thermal stability below 70 C, optimum C Characteristics Matrix: amino acrylic polymer Particle size: μm Water content: 60 70% Storage The enzymatic preparations should be stored between 2 8 C. Recommendations: for a proper use of SPRIN Protease Kit, magnetic stirring should be avoided. We suggest, when working in batch, the following stirring methods: blood-rotator, orbital shaker, mechanical stirrer (recommended 120 rpm). 3
4 Activity assay reaction: The assay is based on the hydrolysis of Casein. Enzyme activity is expressed as U/g, corresponding to the quantity of enzyme that released 1 µmol of L-Tyrosine-equivalent trichloracetic acid soluble peptides per minute at ph 6.5 and 40 C using an initial concentration of casein of 2% w/v. The amount of L-Tyrosine-peptides is detected spectrophotometricaly at 280 nm. SPRIN immobilised SUBTILISIN Examples of application: Protection/deprotection of aminoacids and peptides, by catalysis of ester bond formation. Protection NH R OH Imm. subtilisin Protection NH R O(CH 2 ) n OH O HO(CH 2 ) n OH O H 2 N(AA) n OH Enzymatic ligation Protection NH R O NH(AA) n OH Protection = Boc or peptide chain Synthesis of peptides in low-water systems. Peptide fragments condensation, bioconjugation, and segmented peptide synthesis. Synthesis of glycopeptides. 4
5 Production of hydrolysed protein normally present on the market, for example Casein hydrolysed, Whey protein hydrolysed, Egg white protein hydrolysed. Properties of hydrolysed proteins: - Increase of the solubility (up to 50%). The solubility depends of the Degree of Hydrolysis (DH), and will be higher at higher DH. peptide bond cleaved DH (%) total numberof peptide bonds - Decrease of the viscosity of the protein solution. - Change of the emulsifying properties. - Improvement of the foaming properties. - Decrease of the allergenicity (important in baby food formulations). - Lowering bitterness development during protein hydrolysis. Using SPRIN immobilised SUBTILISIN, enzyme inactivating heat treatment at the end of the process is not required since no protein leaching is observed. 5
6 Residual activity (%) SPRIN S.p.A Stability in Ethanol Solutions: SPRIN immobilised SUBTILISIN are stable at different concentrations of ethanol solutions. This graph indicates the time-stability of the SPRIN imibond SUBTILISIN in Ethanol Absolute, in Ethanol Solution 70% (in 20 mm ph 8.0 potassium phosphate buffer), and in Ethanol Solution 60% (in 20mM ph 8.0 potassium phosphate buffer). Alcohols have been adopted as a disinfectant throughout history, and one of the most common ones used today is ethanol. It is frequently utilised in mixtures, and these mixtures are applied to destroy microorganisms like gram-positive and negative bacteria and viruses, but they are ineffective against protozoa and spore Time (days) Ethanol absolute 70% Ethanol 60% Ethanol 6
7 SPRIN immobilised TERMOLYSIN Examples of application: Synthesis of peptides in anhydrous organic solvents, in water-solvent mixture, solidto-solid systems and aqueous systems with removal of the formed peptide by precipitation. Enzymatic synthesis of aspartame precursor by condensation of Z-Asp and L-phenylalanine methyl ester (PheOMe). Peptide structural analysis, exploiting preferential fragmentation of Leu, Ile, Phe, Val containing peptides. Production of hydrolysed protein normally presented on the market, for example Casein hydrolysed, Whey protein hydrolysed and Egg white protein hydrolysed. Properties of hydrolysed proteins: - Increase of solubility (up to 50%). The solubility depends on the Degree of Hydrolysis (DH), and will be higher at a higher DH. peptide bond cleaved DH (%) total numberof peptide bonds - Decrease of viscosity of the protein solution. - Change of emulsifying properties. - Improvement of foaming properties. - Decrease of allergenicity (important in baby food formulations). - Lowering of the development of bitterness during protein hydrolysis. Operative Stability after Vat Pasteurization treatment (Water at 65 C for 30 minutes) Vat Pasteurization consists of a thermal treatment (60-65 C for 30 minutes) that allows the lowering of bacterial load. This treatment is used to extend the shelf life of foodstuff, while maintaining all the nutritive properties of fresh food, and for this reason is used as a conservative treatment for milk, beer, wine, pudding and fruit juices. Thanks to the thermal stability of SPRIN immobilised THERMOLYSIN preparations, they can undergo many Vat Pasteurization cycles without loss of activity, allowing its re-use i.e. in whey protein hydrolysis process. After 5 cycles of Vat Pasteurization Treatment SPRIN imibond THERMOLYSIN retains 100% initial activity (see below graph). 7
8 Note for use: SPRIN immobilised SUBTILISIN SPRIN immobilised THERMOLYSIN The enzymatic preparations are stored in glycerol/buffer mixture (80% glycerol in 20mM ph 8.0 potassium phosphate) and should be stored at 4 C. They must be washed before use. Three washing cycles ensure complete removal of glycerol. Washing conditions: 4ml of 20mM ph 8 potassium phosphate buffer solution per gram of enzymatic preparation. It is possible to use the Filter (see diagram) for filtration of the glycerol-buffer mixture and washing of the enzymatic preparations. 8
9 After use of the enzymatic preparations a- Wash the enzymatic preparations to remove substrates or products of the enzymatic system (e.i. with potassium phosphate buffer) b- Store the enzymatic preparations in glycerol-buffer mixture (80% glycerol in 20mM ph 8.0 potassium phosphate). Literature: Subtilisin: C. Liu et al., Org. Lett. 2001, 3, J. U. Klein et al., J. Pept. Sci. 2000, 6, 541. T.J. Tolbert et al., Methods in Molecular Biology, 283, 2004: Bioconjugation protocols, strategies and methods, Editor: C.M. Niemeyer, Humana Press, Totowa, NJ. A.V. F.M. Bachevaa et al., Bioorg. & Med. Chem. Lett. 2001, 11, J.C. Hubbs et al., Process for synthesizing peptides - fragment condensation, U.S. Patent , issued on June 21, Thermolysin: A.J. Trusek-Holownia, Biotechnol. 2003, 102, 153. R.V. Ulijn et al., Biotechnol Bioeng. 2000, 69, 633. T. Nagayasu et al., Biotechnol. Bioeng. 1994, 43, A. Basso et al., Chem. Commun. 2000, 467. L. De Martin et al., Tetrahedron Letters 2001, 42, R.L. Heinrikson, Applications of thermolysin in protein structural analysis. Methods in Enzymology, 1977, 47, 175, Elsevier. 9
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