Determination of Lactose Concentration in Low-Lactose and Lactose-Free Milk, Milk Products, and Products Containing Dairy Ingredients, Enzymatic Method: Single-Laboratory Validation First Action Method 2020.08.

Background: The AOAC Stakeholder Panel on Strategic Food Analytical Methods issued a call for methods for the measurement of lactose in low-lactose and lactose-free products under Standard Method Performance Requirement (SMPR®) 2018.009. Megazyme's Lactose Assay Kit (K-LOLAC) was developed specifically to address the need for accurate enzymatic testing in lactose-free samples.

Determination of Ethanol Concentration in Kombucha Beverages: Single-Laboratory Validation of an Enzymatic Method, First Action Method 2019.08.

Kombucha is a fermented, lightly effervescent sweetened black or green tea drink. It is marketed as a functional beverage based on its proposed health benefits. Kombucha is produced by fermenting tea using a "symbiotic colony of bacteria and yeast" (SCOBY).

Ethyl-for-methyl substitution enhances the subtype specificity of mecamylamine analogues.

The synthesis of novel mecamylamine analogues is described in which one, two or three of the methyl groups of mecamylamine have been systematically replaced with ethyl groups. Assessment of the compounds highlights that simple ethyl for methyl changes changes to the parent structure can dramatically enhance activity and selectivity towards either the α4β2 (at the expense of α3β4) or the α3β4 (at the expense of α4β2) nicotinic acetylcholine receptor sub-type as compared to the parent compound.

Novel substrates for the automated and manual assay of endo-1,4-β-xylanase.

endo-1,4-β-Xylanase (EC 3.2.1.

A new synthesis and preliminary evaluation of some analogues of mecamylamine - a compound with anti-addiction properties.

A new synthesis of mecamylamine - a known anti-hypertensive drug with anti-addictive properties is described. The new route allowed access to two novel analogues whose activity at two nicotinic acetylcholine receptor subtypes was assessed.

A novel automatable enzyme-coupled colorimetric assay for endo-1,4-β-glucanase (cellulase).

endo-1,4-β-Glucanase (endo-cellulase, EC 3.2.1.

Hydrolysis of wheat flour arabinoxylan, acid-debranched wheat flour arabinoxylan and arabino-xylo-oligosaccharides by β-xylanase, α-L-arabinofuranosidase and β-xylosidase.

A range of α-L-arabinofuranosyl-(1-4)-β-D-xylo-oligosaccharides (AXOS) were produced by hydrolysis of wheat flour arabinoxylan (WAX) and acid debranched arabinoxylan (ADWAX), in the presence and absence of an AXH-d3 α-L-arabinofuranosidase, by several GH10 and GH11 β-xylanases. The structures of the oligosaccharides were characterised by GC-MS and NMR and by hydrolysis by a range of α-L-arabinofuranosidases and β-xylosidase. The AXOS were purified and used to characterise the action patterns of the specific α-L-arabinofuranosidases.

Novel assay procedures for the measurement of α-amylase in weather-damaged wheat.

Background: The measurement of α-amylase (EC 3.2.1.

Colourimetric and fluorometric substrates for measurement of pullulanase activity.

Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable α- and β-glucosidases and either 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl (1-6) α-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-β-maltotriosyl (1-6) α-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, β-amylase and α-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue.

Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase).

A specific and sensitive substrate for the assay of endo-1,4-β-glucanase (cellulase) has been prepared. The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-β-cellotrioside (BzCNPG3) in the presence of thermostable β-glucosidase. Hydrolysis by exo-acting enzymes such as β-glucosidase and exo-β-glucanase is prevented by the presence of the benzylidene group on the non-reducing end d-glucosyl residue.