Finally, the residue was incubated with amyloglucosidase
at a temperature of 60[degrees]C for 30 min.
was capable of hydrolyzing starches from various botanical sources to produce a porous structure that absorbed and delivered liquid oil into a dry system for bake-only nugget applications.
An aliquot (0.5 mL) of the solution was transferred to a 2 mL tube and 200 pL of amyloglucosidase
(60 U/mL in 0.1 mol/L ammonium acetate, pH 5.5) was added.
The dispersed sample was then subjected to hydrolysis treatment with amyloglucosidase
(14units/mg of protein) (Roche, Indianapolis, IN, USA) and subsequently incubated (60[degrees]C, 45 min, pH 4.75).
A 100-[micro]L portion of the whole-tissue homogenate was neutralized with KOH and incubated with amyloglucosidase
(1 mg [mL.sup.-1]) at 40[degrees]C in a 0.2 M sodium acetate buffer, pH 4.8.
Residues were added to 4 mL of trismaleate/0.1M NaOH (pH 6) containing 0.02% sodium azide, amyloglucosidase
(4U/mL, Sigma Aldrich[R] A 7255), [alpha]-amylase (300U/mL, Sigma Aldrich[R] A-3176), and pepsin (500U/mL, Sigma Aldrich[R] P-7012).
The aim of this work was to produce brandy from cassava peel, through the processes of enzymatic hydrolysis using commercial enzymes (a-amylase, amyloglucosidase
and xylanase), with the aid of the alcoholic fermentation of the yeast Saccharomyces cerevisiae and distillation.
Glycogen was estimated from 50-mg subsamples after extraction with 0.1 M trisodium citrate buffer pH 5.0, conversion to glucose by overnight incubation at room temperature with 0.5% amyloglucosidase
and color development using Trinder reagent (Biotron Diagnostics Inc., Hemet, CA) (Braid et al.
(exo-1-4-[alpha]-D-glucan glucano hydrolase,(EC 18.104.22.168) hydrolyses single glucose unit from non-reducing ends of amylase and amylopectin in stepwise manner.
The precipitate was pelleted by centrifugation (2000 x g; 15 min) and dispersed in DMSO before hydrolyzing with 0.1 ml amyloglucosidase
in 0.1 M acetate buffer (pH 4.6).
We obtained a number of mixtures of proteins with different pI values (IEF MIX-Sigma, USA, pH 3.G-9.3) containing amyloglucosidase
(pI 3.6), trypsin inhibitor (pI 4.G), [beta]-lactoglobulin A (pI 5.1), carbonic anhydrase II (bovine, pI 5.9), carbonic anhydrase I (human, pI 6.6), myoglobin (pI 6.8, 7.2), lectin from Lens culinaris (pI 8.2, 8.G, 8.8), and trypsinogen (pI 9.3); identifications of the different pI values were made using an image densitometer G 700 (Bio-Rad, USA).