Pancreatic trypsin novo 6.0s

Manufactured by Novozymes

Sourced in Denmark

Pancreatic Trypsin Novo 6.0S is a laboratory product manufactured by Novozymes. It is a proteolytic enzyme derived from bovine pancreas. The core function of this product is to catalyze the hydrolysis of peptide bonds in proteins.

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4 protocols using pancreatic trypsin novo 6.0s

Soybean Protein Hydrolysis Using Diverse Enzymes

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Soybeans (Glycine max (L.) merr.) were purchased from Naturkost Ernst Weber (Munich, Germany). Enzymes used in this study including Alcalase^® 2.4 L FG (endoprotease from Bacillus licheniformis), Flavourzyme^® 1000 L (endoprotease and exopeptidase from Aspergillus oryzae), Protamex^® (endopeptidase from Bacillus licheniformis and Bacillus amyloliquefaciens), Neutrase^® 0.8 L (endoprotease from Bacillus amyloliquefaciens), and Pancreatic Trypsin Novo^® 6.0 S (endopeptidase from Porcine pancreatic glands) were kindly provided by Novozymes A/S (Bagsvaerd, Denmark). Papain (cysteine‐protease from papaya latex) (E.C. 3.4.22.2, Sigma no P4762) and Pepsin (endoprotease from Porcine gastric mucosa) (E.C. 3.4.23.1, Sigma no P6887) were purchased from Sigma‐Aldrich Inc. (St. Louis, MO) and Corolase^® 7089 (endopeptidase from Bacillus subtilis), Corolase^® 2TS (endopeptidase from Bacillus stearothermophilus) as well as Protease N‐01 (endoprotease from Bacillus subtilis) were kindly provided by AB Enzymes GmbH (Darmstadt, Germany) and ASA Spezialenzyme GmbH (Wolfenbüttel, Germany), respectively.
All chemicals used in this study were of analytical grade and obtained from Th. Geyer GmbH & Co. KG (Renningen, Germany).

Meinlschmidt P., Sussmann D., Schweiggert‐Weisz U, & Eisner P. (2015). Enzymatic treatment of soy protein isolates: effects on the potential allergenicity, technofunctionality, and sensory properties. Food Science & Nutrition, 4(1), 11-23.

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Enzymatic Characterization of Proteases

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Angiotensin-converting enzyme I (ACE, EC 3.4.15.1), acetonitrile of HPLC grade and trifluoroacetic acid (TFA) were from Sigma Chemical Co. (St. Louis, MO, USA); Prolyl endopeptidase (PEP, EC 3.4.21.26) from Flavobacterium was purchased from Seikagaku Corp. (Tokyo, Japan). The chromogenic substrates (Z-Gly-Pro-7-amido-4-methylcoumarin) and Abz-GLY-PHe(NO2)-Pro were from Bachem Feinchemikalien (Bubendorf, Switzerland). Sigma Chemical Co. (St. Louis, MO, USA) provided porcine kidney Dipeptidyl Peptidase IV (DPP-IV, EC 3.4.14.5) and its chromogenic substrate (H-Gly-Pro-AMC-HBr), hippuryl-His-Leu, angiotensin II, vitamin B12 and aprotinin. Novozymes (Bagsværd, Denmark) kindly provided commercial proteases (Alcalase® 2.4 L, Esperase® 8.0 L, and Pancreatic Trypsin Novo 6.0S). All other analytical grade chemicals were purchased from Panreac Chemical Co. (Barcelona, Spain).

Bougatef H., Sila A., Bougatef A, & Martínez-Alvarez O. (2024). Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides. Marine Drugs, 22(4), 156.

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Enzymatic Hydrolysis of Angiotensin-Converting Enzyme

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Alcalase^® 2.4 L (from Bacillus licheniformis), Pancreatic Trypsin Novo 6.0S, Protease type XIV, also known as Pronase E (from Streptomyces griseus) and Esperase^® 8.0 L (from Bacillus spp.) were obtained from Novozymes (Bagsværd, Denmark). Angiotensin-Converting Enzyme I (ACE, EC 3.4.15.1), aprotinin, vitamin B12, angiotensin II, hippuryl histidyl leucine (HHL) and glycine were obtained from Sigma Chemical Co., (St. Louis, MO, USA). Abz-GLY-PHe(NO₂)-Pro was obtained from Bachem Feinchemikalien (Bubendorf, Switzerland). All other chemicals and reagents used were of analytical grade and were purchased from Panreac Chemical Corp. (Barcelona, Spain).

Bougatef H., de la Vega-Fernández C., Sila A., Bougatef A, & Martínez-Alvarez O. (2023). Identification of ACE I-Inhibitory Peptides Released by the Hydrolysis of Tub Gurnard (Chelidonichthys lucerna) Skin Proteins and the Impact of Their In Silico Gastrointestinal Digestion. Marine Drugs, 21(2), 131.

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Preparation of Caseinates from Goat and Cow Milk

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Goat and cow caseinate were prepared by isoelectric precipitation of reconstituted goat (predominantly Saanen) or cow milk powder obtained from Dairy Goat Co-operative (Hamilton, New Zealand), and Fonterra Co-operative (purchased from Milligans Food Group Ltd., Oamaru, New Zealand), respectively. Briefly, the skim milk powders were hydrated to 10% (wt/wt) and acidified to pH 4.6 for cow and 4.2 for goat milk at 15°C. The solutions were warmed to 30°C and the precipitate collected by centrifugation. The precipitates were caseinated by addition of sodium hydroxide to pH 6.7 and freeze-dried. We obtained ammonium bicarbonate, ammonium molybdate, disodium tetraborate, and sodium sulfite from BDH Chemicals (Poole, UK); hydrochloric acid, sodium hydroxide, 2-propanol, acetonitrile, trifluoroacetic acid, and ferrous sulfate from Fisher Scientific (Leicestershire, UK); hydrogen peroxide, disodium EDTA, and sodium chloride from LabServ (Biolab, Australia); o-phthaldialdehyde (OPA), dithiothreitol, serine, ferrozine, and neocuprione from Sigma (St. Louis, MO); Eriochromeback T indicator from Riedel-de Haën (Seelze, Germany); and trypsin (Pancreatic Trypsin Novo 6.0S) from Novozymes (Bagsvaerd, Denmark). All water was MilliQ grade, and all other chemicals were analytical grade. The spectrophotometer used throughout was Pharmica UV/visible Ultrospec II (LKB, Biochem, Cambridge, UK).

Smialowska A., Matia-Merino L, & Carr A.J. (2017). Assessing the iron chelation capacity of goat casein digest isolates. Journal of dairy science, 100(4).

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