SERINE PROTEASE WITH CHYMOTRYPSIN SPECIFICITY FROM NOCARDIOPSIS PRASINA EXPRESSED IN BACILLUS LICHENIFORMIS
New specifications prepared at the 76th JECFA (2012) and published in FAO JECFA Monographs 13 (2012). An ADI “not specified” was
established at the 76th JECFA (2012)
SYNONYMS
SOURCES
Chymotrypsins A and B; α-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; α-chymar; α-chymotrypsin A; α-chymotrypsin
Produced by submerged fermentation of a genetically modified non-pathogenic and non-toxigenic strain of Bacillus licheniformiswhich contains a gene coding for serine protease with chymotrysin specificity from Nocardiopsis prasina. The enzyme is secreted to the broth. The cell mass and other solids are separated from the broth by vacuum drum filtration or centrifugation. Ultrafiltration and/or evaporation are applied for concentration and further purification. Residual production strain microorganisms are removed by germ filtration. The final product is formulated using food-grade stabilizing and preserving agents and is standardized to the desired activity.
Active principles Serine protease with chymotrypsin specificity
Systematic names and numbers
beta-Glucanase: EC 3.4.21.1, CAS number: 9004-07-3 Xylanase: 1,4-
CAS number:
Reactions catalysed Preferential cleavage: Tyr, Trp, Phe, Leu
Secondary enzyme activities None
DESCRIPTION Brown liquid
FUNCTIONAL USES Enzyme preparation.
Used in the hydrolysis of proteins like casein, whey, soy isolate, soy concentrate, wheat gluten and corn gluten in the production of partially or extensively hydrolyzed proteins of vegetable and animal origin.
GENERAL SPECIFICATIONS
Must conform to the current edition of JECFA General Specifications and Considerations for Enzyme Preparations Used in Food Processing.
