Beta, Rooney & Waniska 1995: Malting Characteristics of 16 Sorghum Cultivars
This is an external paper. The record of authority is Beta, T., Rooney, L.W. & Waniska, R.D., Malting Characteristics of Sorghum Cultivars, Cereal Chemistry 72(6):533–538 (1995), published by the AACC — publisher's archive PDF. No DOI exists for this back-issue paper. The figures on this page come from the published abstract; this page adds the brewing-side reading and reproduces no tables.
What the study did
Sixteen sorghum cultivars were malted under a germinator method (with six of them also malted by a jar method for comparison), and the malts were analyzed for diastatic power (SDU basis), α-amylase activity, and malting loss. It is the same experimental shape as this site's USDA Madison screening — many named cultivars, one standardized schedule — from an independent lab, three decades earlier.
What it reports
- α-amylase activity ranged from 25 to 183 U/g across cultivars by colorimetric assay — a roughly seven-fold spread from one malting method.
- Two cultivars reached α-amylase activity similar to a commercial barley malt.
- Diastatic power (SDU) correlated positively with α-amylase activity.
- The jar method produced malts with dry-matter losses of 8–19%.
What these numbers mean for brewing
- Cultivar choice moves the enzyme numbers — a lot. A seven-fold α-amylase spread from a single malting schedule is the same lesson the Madison screening taught with extract (31–68%) and DP (19–46 ASBC): "sorghum" is not a specification, and naming the cultivar is the only way any malting result means anything.
- The honest wrinkle: α can get close to barley. Total conversion cannot — so far. Two cultivars matching commercial barley malt on α-amylase is the strongest published data point for native sorghum enzyme potential, and this site states it deliberately. Read it beside Muoria 1998: total diastatic power — which needs the β-amylase side sorghum malt lacks — still ran roughly 27-fold below barley. α-amylase liquefies; saccharification needs the rest of the enzyme system. A cultivar strong on α is a genuinely interesting malting material and still not a self-converting one.
- This is why the doctrine says "no assigned job" instead of "no activity." The site's external-enzymes position has always acknowledged that native activity is real and measurable — this paper is part of why. What no published study yet shows is a cultivar-plus-malting combination reliable enough, lot to lot, to plan conversion around. That exact gap is Research Ask 9, and a result closing it is a named trigger in the position's "what would change our position" record.
Honest limits
Abstract-level extraction: units matter here more than usual — α-amylase in U/g by colorimetric assay and DP on the SDU basis do not convert casually to the ASBC degrees used in Muoria 1998 or the Madison screening; compare shapes and ratios across studies, not raw numbers. The cultivars are 1990s Texas-program materials, not today's commercial hybrids. And α-amylase parity with barley malt on two cultivars is a bench finding about one enzyme class, not a brewing trial — no wort, fermentation, or beer data backs it.