Rational shift of the optimum pH toward alkalinity and enhancement of thermostability were investigated by using a thermostable extremely alkaline protease (optimum pH, 12 to 13) from the alkaliphilic and thermophilic Bacillus sp. strain B18'. The protease gene (aprM) was cloned, and the sequence analysis revealed an open reading frame of 361 amino acids that was composed of a putative signal s...

alkaline protease enzyme produced from bacillus licheniformis ptcc1331 in optimum condition(temperature 37 ?c, 150 rpm, ph=10), is immobilized in different concentrations of sodium alginate using entrapment method, to increase its thermal resistance in detergents, and its activity is measured thereafter. maximum enzymatic activity of 46 was obtained in 2%w/v sodium alginate solution. investigat...

Extracts and culture supernatant solutions of Bacillus Zicheniformis contain considerable quantit.ies of a protease, shown by Bernlohr and Novelli (I) to appear in the extracellular medium only in the postlogarithmic phase of growth. From genetic studies on sporulation in Bacilli, Spizizen, Reilly, and Dahl (2) report a strong association between a protease, formed in the postlogarithmic growth...

Extracts and culture supernatant solutions of Bacillus Zicheniformis contain considerable quantit.ies of a protease, shown by Bernlohr and Novelli (I) to appear in the extracellular medium only in the postlogarithmic phase of growth. From genetic studies on sporulation in Bacilli, Spizizen, Reilly, and Dahl (2) report a strong association between a protease, formed in the postlogarithmic growth...

The granule fraction of human leukocytes contains neutral protease capable of degrading the noncollagenous protein mucopolysaccharide matrix of cartilage at neutral pH in physiological salt solution. Cartilage degradation was monitored by quantitating the release of (35)S from labeled rabbit ear cartilage. Degradation of cartilage matrix occurs when intact viable human leukocytes are incubated ...

An integral membrane protease was solubilized and purified to homogeneity from rat submaxillary mitochondria. The purified enzyme could coagulate rabbit plasma. The molecular mass of the enzyme is 22 kDa on SDS-polyacrylamide gel electrophoresis under reducing conditions and 24 kDa on gel filtration on a Sephadex G-100 column. Its isoelectric point is 4.2-4.25. Enzyme activity is strongly inhib...

The dimeric nature of the HIV protease has been exploited to devise a novel mode of inhibiting the enzyme. The use of defective monomers or nonidentical subunits to exchange with wild-type homodimers produces catalytically defective heterodimers. Incubation of the HIV1 or HIV2 protease with a 4-fold molar excess of an inactive mutant of HIV1 leads to 80 and 95% inhibition of enzyme activity, re...