ISSN:
1750-3841
Quelle:
Blackwell Publishing Journal Backfiles 1879-2005
Thema:
Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft
,
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
Susceptibility of the major storage protein, phaseolin, to different commercially available proteinases was studied in vitro for 17 varieties of Phaseolus vulgaris L. using electrophoretic techniques. Among serine proteinases, trypsin, subtilisin and pronase E readily hydrolyzed the native phaseolin. while chymotrypsin was less effective. Native phaseolin was markedly resistant to a carboxyl proteinase (pepsin) and somewhat resistant to a thio proteinase (papain). Major breakdown products of native phaseolin subunits were of a similar size irrespective of the enzyme used. and had an approximate MW of 22–25 kilodaltons. SDS-PAGE indicated that heated phaseolin from all the varieties investigated was effectively hydrolyzed by subtilisin, pronase E. pepsin and papain within 30 min, while chymotrypsin and trypsin exhibiting restricted specificity were slightly less effective.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1111/j.1365-2621.1987.tb14074.x
Permalink
