Skip to main content
AMERICAN SOCIETY OF
BREWING CHEMISTS

DEI Image
Join | Renew | Contact | Log In
Search
  • About
    • Research Council
    • Directories
    • DEI Resources
    • Social Media Kit
    • Contact Us
  • Membership
    • My ASBC Account
    • Join
    • Renew
    • ASBC Connect Community
    • Job Center
    • Student Resources
    • Awards
    • Volunteer
    • Apply for Funding
    • Corporate Membership
  • Methods
    • Methods of Analysis
    • About
    • Tools
    • FAQ
    • Subscription Options
  • In the Lab
    • Methods Videos
    • Lab Proficiency Program
    • Reference Materials and Gauges
    • Fishbone References
    • Grow Your Own Lab
    • Sensory Analysis
    • Sampling Plan
    • Green Chemistry
  • PublicationsCurrently selected
    • Journal
    • Books
    • Technical Committee Reports
    • Advertise
  • Events
    • Brewing Summit 2025
    • Webinars
    • WBC Rewind
    • Meeting Archives
  • Store
Skip navigation links
2017
2016
2015
1977-2014
American Society of Brewing ChemistsPublicationsJournalVolume Years2016

Display Title
Maltose Effects on Barley Malt Diastatic Power Enzyme Activity and Thermostability at High Isothermal Mashing Temperatures: II. α-Amylase (1)






Page Content
​This study was conducted to determine if maltose, the primary product of starch degradation during mashing, would affect the activity of or increase the thermostability of barley malt α-amylase activity at high temperatures used in mashing and temperatures above those normally used in mashing. Malts of the two-row cultivar Harrington and the six-row cultivar Morex were mashed for 2 h with maltose concentrations of 0–500 mM at temperatures from 63 to 78°C. Worts were sampled every 30 min for 120 min and α-amylase activities determined utilizing the Megazyme Ceralpha assay. Mannitol, a polyhydric alcohol, was used for comparison. Polyhydric alcohols are known to enhance enzyme thermostability. At 63°C both cultivars had relatively thermostable α-amylase without the addition of maltose or mannitol. However, Morex, and to a lesser extent Harrington, α-amylase activity was significantly elevated by high levels of either maltose or mannitol, indicating a stimulatory effect on activity in which thermostability was apparently not involved. At 73 and 78°C increasing concentrations of maltose conferred considerable and highly significant (LSD analysis, P < 0.0001) thermal protection of α-amylase in both cultivars. For example, at 30 min of mashing at 73°C, maltose concentrations of 400 and 500 mM resulted in α-amylase activity in Harrington of 227 and 252% and in Morex 349 and 314%, respectively, of the 0 mM maltose activity. At 60 min of mashing at 73°C, concentrations of 400 and 500 mM maltose resulted in α-amylase activities of Harrington of 290 and 431% and Morex of 489 and 501%, respectively, of the 0 mM maltose activity. High mannitol incubations at higher temperatures such as at 73°C rendered lesser α-amylase thermal protection than maltose; however, it was also considerable and highly significant (P < 0.0001) for both cultivars (e.g., 30 min incubation at 73°C, with 400 and 500 mM maltose, respectively, α-amylase activities of Harrington were 163 and 174% and Morex were 188 and 260% of the 0 mM maltose activity). These data suggest that the production of maltose, as could be expected in high-gravity mashes, significantly increases the activity and thermostability of barley malt α-amylase. Keywords: α-Amylase, Barley, Enzyme thermostability, Maltose, Mannitol, Mashing

About

Join

Contact

Advertise

Privacy Policy

Email Deliverability