Tritirachium album

Tritirachium album derived proteinase K P-lg IPA Antihypertensive Abubakar et al. (1998)... 

After the introduction of pronase E, other more or less nonsubstrate-specific proteolytic enzymes have been applied to assist Se speciation. Most of them were derived from DNA/RNA clean-up protocols. The new enzymes (subtilisin from Bacillus licheniformis, also named protease VIII, EC 3.4.21.14 proteinase K from Tritirachium album, EC 3.4.21.64 the crude Novo Nordisk product of Flavourzyme from Aspergillus oryzae) proved to be capable of extracting Se with varying yields and chromatographic recovery of Se species. It is important to highlight that the latter parameter also depends on the instrumentation available. In this regard, different recovery values for the same samples reported by independent research groups do not necessarily indicate successful or unsuccessful sample preparation. Similarly, extraction efficiency (defined as the ratio of extracted Se to total Se in the sample) cannot be used as such for comparison purposes because sample preparation may include some extra steps, for example, TCA precipitation or ultrafiltration, which may reduce this value even by 10-20 percent. 

Proteinase K, immobilized on EupergitC Origin Tritirachium album... 

Betzel, C., Gourinath, S., Kumar, P., Kaur, P., Perbandt, M., Eschenburg, S., Singh, T.P., 2001. Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 A resolution. Biochemistry 40, 3080—3088. 

Williams reported the enzymatic hydrolysis of poly(L-lactic acid) (PLLA) in the presence of enzymes such as pronase, proteinase K, and bromelain. However, these enzymes are proteases and not PLLA depolymerases [3]. Regarding PLA stereocopolymers, Fukuzaki et al. reported that the hydrolysis of PLA was accelerated in the presence of specific enzymes and the most rapid enzymatic degradation of the stereocopolymers was observed on the poly(DL-lactic acid) (PDLLA) sample containing 50% L-lactic acid (LLA) [4]. Furthermore, Makino et al. showed that the addition of a carboxylic esterase accelerated a decrease in the weight-average molecular weight of PDLLA [5]. Reeve et al. reported the effects of stereochemical composition on enzymatic degradability of PLA films by proteinase K from Tritirachium album [6]. 

For this study we chose to modify the activity, pH optimum and thermostability of the enzyme proteinase K from Tritirachium album. Hydrolytic enzymes such as proteases and lipases are finding many applications in polymer synthesis and degradation (74-27). The activity and physical properties of these enzymes determine whether or not they will make suitable biocatalysts for polymer modifrcation. 

Cloning of the proteinase K from Tritirachium album Umber and expression of the active protease has been described (22). We did not attempt to obtain a sample of the cloned gene this path is often fraught with difficulties and delays and can even result in significant work being expended on a construct that ultimately reveals itself to be an imposter. Instead we decided to synthesize... 

Tritirachium album ATCC 22563 Protease L-PLA, silk fibroin, elastin Film-weight loss monomer production (lactic acid)... 

However, a PrPp forces the pathogenic conformation on a PrPn. The stability towards serine proteinase K from the fungus Tritirachium album is used to differentiate between PrPp and PrPn. Serine proteinase K, which attacks the carboxyl side of hydrophobic amino acids, largely hydrolyzes PrPn while a characteristic peptide (M 27-30 kDa) is released from PrPp. This marker can be identified using the sandwich ELISA (cf. 2.6.3). 

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