Search Results

You are looking at 1 - 10 of 90 items for :

  • All content x
Clear All

. Kakade , M.L. , Rackis , J.J. , Mcghee , J.E. & Puski , G. 1974 : Determination of trypsin inhibitor activity of soy products: A collaborative analysis of an improved procedure . Cereal Chem. , 51 , 376 – 382

Restricted access
Acta Chromatographica
Authors: Amanda Fernandes de Medeiros, Maria Gabriela Ferreira Rocha, Alexandre Coelho Serquiz, Richele Janaína Araújo Machado, Vanessa Cristina Oliveira Lima, Fabiana Maria Coimbra de Carvalho, Izael de Sousa Costa, Bruna Leal Lima Maciel, Elizeu Antunes dos Santos, and Ana Heloneida de Araújo Morais

be attributed to the presence of a trypsin inhibitor [ 11 , 12 ]. In fact, there are studies that confirm the presence of various enzymatic trypsin inhibitors in different peanut varieties [ 13 – 16 ], as well as in their derived food products

Open access

Veličković, D., Vucelić-Radović, B., Barać, M. & Simić, D. (1992): The change of trypsin inhibitor activity as a function of pressure and the duration of thermal treatment of soybean flour. Rev. Res. Work Fac. Agric., 37 , 109

Restricted access
Acta Microbiologica et Immunologica Hungarica
Authors: L. Kredics, Zsuzsanna Antal, A. Szekeres, L. Manczinger, Ilona Dóczi, F. Kevei, and Elisabeth Nagy

Species belonging to the filamentous fungal genus Trichoderma are well known as potential candidates for the biological control of plant pathogenic fungi and as cellulase producers of biotechnological importance. Several data were published in the last decade also about the clinical importance of this genus, indicating that Trichoderma strains may be potential opportunistic pathogens in immunocompromised patients. However, there is a lack of information about the potential virulence factors of clinical Trichoderma strains. This study was designed to examine the extracellular proteolytic enzymes of six clinical T. longibrachiatum isolates. Supernatants from induced liquid cultures of the examined strains were screened for proteolytic enzyme activities with 11 different chromogenic p-nitroaniline substrates. The production of trypsin-like, chymotrypsin-like and chymoelastase-like protease activities cleaving N-Benzoyl-L-Phe-L-Val-L-Arg-p-nitroanilide, N-Succinyl-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide,and N-Succinyl-L- Ala-L-Ala-L-Pro-L-Leu-p-nitroanilide, respectively, was common among the strains examined. Separation of trypsin- and chymotrypsin-like activities by column chromatography revealed, that both systems are complex consisting of several isoenzymes. The pH-dependence of these two protease systems was also studied. Based on the results, the different isoenzymes seem to have different optimal pH values. Extracellular proteolytic enzymes may be involved in the pathogenecity of Trichoderma strains as facultative human pathogens.

Restricted access

Abstract  

Optimum temperature and pH for the isolation of soy protein isolate (SPI) from soy protein concentrate (SPC) were established. Enzymatic hydrolysis of SPI with enzymes of different specificities such as trypsin, chymotrypsin, papain and urease was carried out and the products of hydrolysis were characterized by molecular mass determination [sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)] and thermal techniques [differential scanning calorimetry (DSC) and thermogravimetric analysis (TG)]. Enzymatic hydrolysis resulted in a significant reduction in molecular masses. However the thermal stability of hydrolysed SPI was similar to native SPI indicating that it is independent of molecular mass. DSC studies indicated an increase in temperatures of endothermic transition associated with SPI denaturation and loss of absorbed moisture in samples of lower molecular masses.

Restricted access
Acta Microbiologica et Immunologica Hungarica
Authors: L. Kredics, Zsuzsanna Antal, A. Szekeres, L. Hatvani, L. Manczinger, Cs. Vágvölgyi, and Erzsébet Nagy

Uchikoba, T., Mase, T., Arima, K., Yonezawa, H., Kaneda, M.: Isolation and characterization of a trypsin-like protease from Trichodermaviride. Biol Chem 382 , 1509-1513 (2001). Isolation and characterization of a trypsin

Restricted access

433 438 Bhatty, R. S. (1988): In vitro hydrolysis of pea, faba bean and lentil meals and isolated protein fractions by pepsin and trypsin. Can. Inst. Fd Sci. Technol , 21 , 66

Restricted access

Birk, Y. (1961): Purification and some properties of a highly active inhibitor of trypsin and chymotripsin from soybeans. Biochem. Biophys. Acta , 54 , 378

Restricted access

1317. Gee, Y. Y. C. and Morgan, R. G. H. (1993): The effect of trypsin inhibitor on the pancreas and small intestine in mice. Br. J. Nutr. 7, 333-345. The effect of

Restricted access
Orvosi Hetilap
Authors: Miklós Sahin-Tóth, Péter Hegyi, and Miklós Tóth

Király, O., Wartmann, T., Sahin-Tóth, M.: Missense mutations in pancreatic secretory trypsin inhibitor (SPINK1) cause intracellular retention and degradation. Gut, 2007, 56 , 1433

Restricted access