EC Number   |
Application |
Reference |
|---|
   3.4.21.96 | biotechnology |
conversion of lactocepin substrate binding regions by allele exchange can effectively alter lactocepin specificity in industrial strains of Lactococcus lactis without significantly affecting other important strain properties. The methodology can be used to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect |
665338 |
| 3.4.21.96 | food industry |
CEP isolated from Mongolian fermented mare's milk strain SBT11087 is distinct from those from previously reported Lactobacillus helveticus strains in terms of its optimal temperature and its degradation of beta-casein |
-, 753888 |
| 3.4.21.96 | industry |
method to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect. PrtP derivatives developed by this approach should be suitable for commercial applications in the US and other countries with a favourable regulatory climate |
-, 665338 |
| 3.4.21.96 | more |
exposure of PrtP, and not its proteolytic activity, is responsible for greater cell hydrophobicity and adhesion. The increased bacterial affinity to polar and apolar solvents indicates that exposure of PrtP on lactococcal cell surface can enhance the capacity to exchange attractive van der Waals interactions, and consequently increase their adhesion to different types of solid surfaces and solvents. PrtP or its derivatives may be used as a tool to construct strains with increased adhesion that form protective biofilms |
685827 |
| 3.4.21.96 | nutrition |
cheese making, cheese starter organism, dairy industry |
29890, 649355 |
| 3.4.21.96 | synthesis |
optimisation of enzymatic hydrolysis of beta-casein to produce the angiotensin-I-converting enzyme (ACE) inhibitory peptides. Under optimal conditions (enzyme-to-substrate ([E]/[S]) ratio (w/w) of 0.132 and pH of 8.00 at 38.8°C), the ACE inhibitory activity of hydrolysates is 72.06% and the total peptides is 11.75 mg/ml. The resulting hydrolysates have higher thermal stability than beta-casein and show an increase in the free sulfhydryl content compared with raw beta-casein |
-, 753892 |
