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'Inhibitor' in keywords Facet   Publication Year 1997  [X]
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1997[X]
1Author    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