Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang

Article Abstract:

The Bacillus sp. strain CK 11-4 isolated from the fermented soybean sauce Chungkook-Jang produces a fibrinolytic enzyme (CK) that exhibits hydrophilic, fibrinolytic and thermophilic activity. The molecular weight of CK is 28,200, optimum temperature is 70 degrees C and optimum pH is 10.5. The initial 14 amino acids of the N-terminal are identical in CK and subtilisin Carlsberg. However, the substrate specificity and level of enzymatic activity of the enzymes are different. Fibrinolytic activity increases when CK is added to a plasminogen and substrate mixture even though plasminogen remains inactive.

Composition, Fibrinolytic agents, Fermented foods, Thrombolytic drugs

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Hydrolysis of feather keratin by immobilized keratinase

Article Abstract:

The Bacillus licheniformis keratinase immobilized on glass beads exhibits proteolytic activity against insoluble feather keratin and soluble casein. The keratinase is more stable, and resistant to high temperature and high-acidic conditions in contrast to free keratinase. The immobilized keratinase converts ground feathers to peptides and amino acids, which are separated by filtration or ion-exchange chromatography. The binding ability of the keratinase is low.

Observations, Hydrolysis

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Stabilization and microbial cytochrome P-450 activity by creation of stationary-phase conditions in a continuously operated immobilized-cell reactor

Article Abstract:

Experimental studies to develop a technique for the stabilization of microbial cytochrome P-450 monooxygenase activity reveal that proper combination of reactor design, medium composition and cell immobilization enables the continuous stimulation of physiological condition. This stimulation is vital for stabilizing the continuous 15 beta-steroid hydroxylation catalyzed by Cyt P-450.

Cytochrome P-450

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