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Kirkpatrick and Shellhammer (2018) found that the enzymes responsible for the conversion of dextrins into sugars include amyloglucosidase (removes glucose from non-reducing ends of α-1,4 and branching α-1,6 linkages, with a preference for α-1,4 linkages and longer chain oligosaccharides), α-amylase (hydrolyzes randomly along glucopolysaccharides to produce maltose, maltotriose, maltopentaose, and maltohexaose products from amylose as well as maltose, glucose, and branched dextrins from amylopectin), β-amylase (saccharifiying enzyme, cleaving maltose in small amounts from nonreducing ends of glucopolysaccharides, and to a minor extent, maltotriose), and limit dextrinase (debranches limit dextrins at α-1,6 linkages, producing linear α-1,4 chains which can further be degraded by the combined action of amylases). They were able to successfully extract them from Cascade pellet hops using commercially available assays (enzyme specific para-nitrophenyl blocked oligosaccharide substrates). The amount of α and β-amylase found in Cascade hops was well below that of malted barley, but within the range reported in other plant leaves. These enzymes are denatured by high temperatures, and as such would be denatured when boiling hops. They reported a similar increase in ABV of 1.3% after 40 days when dry hopping a beer with Cascade hops (and a decrease of 1.9°P) at a rate of 10 g/L. They also found that the hops contained glucose and a small amount of fructose, which accounted for a sugar increase of 0.02−0.03 °P per gram of hops. More studies on whether or not the amount of dry hopping has a large effect needs to be done, and whether or not warmer temperatures speed up the enzymatic breakdown of dextrins, and the authors hypothesized that the rate of dextrin break down could be slowed by dry hopping at lower temperatures <ref name="Kirkpatrick_2018">[https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.8b03563 Evidence of Dextrin Hydrolyzing Enzymes in Cascade Hops (Humulus lupulus). Kaylyn R. Kirkpatrick and Thomas H. Shellhammer. 2018. DOI: DOI: 10.1021/acs.jafc.8b03563.]</ref>.

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