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1997 (1)
1985 (1)
1Author    Akira Taketo, Yoriko TaketoRequires cookie*
 Title    Enhanced Production of Cell-Bound and Extracellular Streptolysin S by Hemolytic Streptococci Pretreated with Proteases  
 Abstract    The amount o f streptolysin S produced by resting streptococci was considerably increased after incubation o f the washed bacteria with trypsin or pronase. Production o f both cell-bound and free forms o f the toxin was enhanced by the protease treatment. By addition o f trypsin, streptolysin S yield was considerably increased in growing culture as well. Treatment with lysozyme was ineffective, and the toxin production was only slightly prom oted by preincubation with hyaluronidase or Chymotrypsin. In contrast, pretreatment with chymotrypsin caused in­ creased production o f an extracellular nuclease, whereas the yield o f this enzyme was reduced after incubation o f the cocci with pronase. Evidence was obtained indicating de novo synthesis o f the exotoxin in the protease-treated bacteria. 
  Reference    Z. Naturforsch. 40c, 166 (1985); received N ovem ber 22 1984 
  Published    1985 
  Keywords    Streptolysin S, Cell-Bound Hemolysin, Protease, Streptococci 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0166.pdf 
 Identifier    ZNC-1985-40c-0166 
 Volume    40 
2Author    M.-L Heskamp, W. BarzRequires cookie*
 Title    Characterization of Proteases from Rhizopus Species after Growth on Soybean Protein  
 Abstract    Culture filtrates of different fungi of the genus R hizopus forming tem pe (i.e. traditional Indonesian food) were grown on a soybean protein-raffinose-phytate medium and investi­ gated for protease activity using soyprotein as substrate. A ll isolates belonging to the species R. oryzae, R. stolonifer, R. oligosporus, and R. m icrosporus var. chinensis, formed the well-known R hizopus-pepsin (aspartic proteinase, 35 kD, isoelectric points: 5.9, 5.0, <4) and an additional protease mainly active under alkaline conditions. The new protease (33 kD, iso­ electric points: variable and isolate specific) was purified approximately 300-fold and shown to be a serine protease (inhibitor studies). During fungal culture (1 2 -1 3 5 h) the aspartic proteinase is expressed first followed by the serine protease. Both proteases are insensitive to the soybean Kunitz and Bowman-Birk inhibitors. The best rate of soyprotein degradation is achieved by the coordinate action of both proteases at pH 6.5. The examined R hizopus isolates differ in the time course and intensity o f the expression o f the alkaline protease. 
  Reference    Z. Naturforsch. 52c, 595 (1997); received May 6/July 3 1997 
  Published    1997 
  Keywords    Soyprotein, R hizopus, Proteases, Tempe, Inhibitors 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0595.pdf 
 Identifier    ZNC-1997-52c-0595 
 Volume    52