Skip to main content
ARS Home » Midwest Area » Madison, Wisconsin » Cereal Crops Research » Research » Publications at this Location » Publication #58471
Title: PURIFICATION AND CHARACTERIZATION OF TWO NEWLY IDENTIFIED CYSTEINE ENDOPROTEINASES FROM GREEN MALT

Author
item Jones, Berne
item ZHANG, NINGYAN - UNIVERSITY OF WISCONSIN
item FONTANINI, DEBORA - UNIVERSITY OF PISA, ITALY

Submitted to: American Society of Brewing Chemists Newsletter
Publication Type: Abstract Only
Publication Acceptance Date: 3/30/1995
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Germinating barley seed endoproteinases regulate the hydrolysis of barley storage proteins during malting, and thus are critical for the malting and brewing processes. In order to define this system so that we can more scientifically design barleys having improved malting quality, we have been studying the endoproteinases of germinating barleys and their endogenous inhibitors. In this presentation we present data on two cysteine endoproteinases that we have recently purified. One (the 31 kD proteinase) has been well characterized and is similar in many ways to the 30 kD endoproteinase we reported several years ago. It's hydrolytic specificity is similar to, but not identical with, that of the 30 kD enzyme. The specificities of both the 30 and 31 kD proteinases are optimal for hydrolyzing hordeins, the predominant storage proteins of barley. The second endoproteinase is larger, is located in the endosperm of green malt and has pH characteristics indicating it may also play a major role in storage protein hydrolysis during malting.