Isolation and characterization of novel tyrosinase from Laceyella sacchari.

We here describe the isolation and characterization of a tyrosinase from a newly isolated soil bacterium. 16S rDNA sequence analysis revealed that the bacterium most probably belongs to the species Laceyella sacchari (Ls) ( > 99.9 % identity).

Debittering of Protein Hydrolysates by Lactobacillus LBL-4 Aminopeptidase.

Yoghurt strain Lactobacillus LBL-4 cultivated for 8-10 h at pH ~6.0 was investigated as a considerable food-grade source of intracellular aminopeptidase. Cell-free extract manifesting >200 AP U/l was obtained from cells harvested from 1 L culture media.

Preparation of antioxidant enzymatic hydrolysates from honeybee-collected pollen using plant enzymes.

Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.

Physicochemical characteristics of a thermostable gellan lyase from Geobacillus stearothermophilus 98.

A purified thermostable gellan lyase, produced by a thermophilic bacterium, Geobacillus stearothermophilus 98, was characterized in relation to its physicochemical properties. The gellan lyase was established to have a molecular weight of 216 kDa, defined by capillary gel electrophoresis. Amino acid analysis revealed high quantities of Lys, His, Ala, Val, Ile, Glx, and Pro residues.

Purification and characterization of tyrosinases from Streptomyces albus.

The bacterium Streptomyces albus has so far never been investigated for tyrosinase activity. The studies presented in this communication show that this bacterium may be a future source for larger production of tyrosinase. The enzyme was purified starting with 5,600 ml of culture filtrate.