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"[This book covers the connection between algebraic K-theory and Bökstedt, Hsiang and Madsen's topological cyclic homology and proves that the difference between the theories are ‘locally constant’. The usefulness of this theorem stems from being more accessible for calculations than K-theory, and hence a single calculation of K-theory can be used with homological calculations to obtain a host of ‘nearby’ calculations in K-theory. For instance, Quillen's calculation of the K-theory of finite fields gives rise to Hesselholt and Madsen's calculations for local fields, and Voevodsky's calculations for the integers give insight into the diffeomorphisms of manifolds. In addition to the proof of the full integral version of the local correspondence between K-theory and topological cyclic homology, the book provides an introduction to the necessary background in algebraic K-theory and highly structured homotopy theory; collecting all necessary tools into one common framework. It relies on simplicial techniques, and contains an appendix summarizing the methods widely used in the field. , This book covers the connection between algebraic K-theory and Bökstedt, Hsiang and Madsen's topological cyclic homology and proves that the difference between the theories are ‘locally constant’. The usefulness of this theorem stems from being more accessible for calculations than K-theory, and hence a single calculation of K-theory can be used with homological calculations to obtain a host of ‘nearby’ calculations in K-theory. For instance, Quillen's calculation of the K-theory of finite fields gives rise to Hesselholt and Madsen's calculations for local fields, and Voevodsky's calculations for the integers give insight into the diffeomorphisms of manifolds. In addition to the proof of the full integral version of the local correspondence between K-theory and topological cyclic homology, the book provides an introduction to the necessary background in algebraic K-theory and highly structured homotopy theory; collecting all necessary tools into one common framework. It relies on simplicial techniques, and contains an appendix summarizing the methods widely used in the field. ]"

"Studi tentang aktivitas protease kasar dari isolat aktinomisetes CiIA5b-DW dan L88b-DW dilakukan menggunakan substrat azocasein. Hasil studi menunjukkan aktivitas protease spesifik tertinggi terjadi pada fase eksponensial (jam ke-16) sebesar 143,993 U/mg untuk isolat CiIA5b-DW dan pada akhir fase stasioner (jam ke-40) sebesar 36,862 U/mg untuk isolat L88b-DW. Ekstrak kasar enzim diambil pada jam dengan aktivitas tertinggi untuk dikarakterisasi. Protease dari isolat CiIA5b-DW mencapai aktivitas tertinggi pada pH 9, suhu 60°C pada kisaran suhu uji 30-60°C, dan dengan penambahan ion logam Ca2+ dan Fe2+ 5 mM, sedangkan protease dari isolat L88b-DW mencapai aktivitas tertinggi pada pH 9, suhu 50°C, serta dengan penambahan ion logam Mg2+ 5 mM. Penambahan EDTA 5 mM mampu menghambat aktivitas protease dari kedua isolat. Nilai Km dan vmax protease dari isolat CiIA5b-DW dan L88b-DW secara berturut-turut ialah 5,687 mM, 0,057 U/menit, 18,034 mM, dan 0,092 U/menit. Berdasarkan hasil penelitian, disimpulkan bahwa protease dari isolat CiIA5b-DW lebih potensial dibandingkan protease dari isolat L88b-DW.

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A study on crude protease activity from actinomycetes isolates CiIA5b-DW and L88b-DW has been carried out using azocasein as substrate. The highest specific activity (143,993 U/mg) of CiIA5b-DW was observed at the exponential phase (16 h) while the highest activity (36,862 U/mg) of L88b-DW was observed at the end of stationary phase (40 h). The enzyme has optimum activity at pH 9 and temperature 60°C for CiIA5b-DW and 50°C for L88b-DW in the temperature range of 30-60°C. The enzyme from CiIA5b-DW was induced when treated with Ca2+ and Fe2+ 5 mM, whereas the enzyme from L88b-DW was induced when treated with Mg2+ 5 mM. The CiIA5b-DW and L88b-DW enzyme inhibited by EDTA 5 mM. Value of Km and vmax of CiIA5b-DW and L88b-DW was 5,687 mM, 0,057 U/min, 18,034 mM, and 0,092 U/min, respectively. Result showed that protease from CiIA5b-DW is more potential than protease from L88b-DW."