*2.1. Cranberry Pomace*

The cranberry pomace was kindly donated by the company "I˛vairios sultys" (Kedainiai, ˙ Lithuania). The moisture content was 3.96%. The pomace was ground to a particle size of 0.5 mm and stored at 4 ◦C.

### *2.2. Proximate Composition Analysis of Cranberry Pomace*

The moisture content was determined by drying 1 g of cranberry pomace in an oven at 105 ◦C to a constant weight, according to the Association of Official Analytical Collaboration (AOAC) Method 925.10-1925. After drying, the final weight of the pomace was subtracted from the initial weight divided by the weight of the sample multiplied by 100 and expressed as g/100 g. The proteins were determined on 1 g of pomace by the Kjeldahl method ( N × 6.25), according to the AOAC Method 978.04. The results were expressed as g/100 g of the dry weight sample. The lipids were determined on 1 g of pomace by drying the sample and subsequently the Soxhlet extraction with hexane was performed for 5 h, according to the AOAC Method 948.22. After the extraction, the residues were dried in an oven at 105 ◦C to a constant weight. The lipid content was calculated from the initial dry weight of pomace by subtracting the final weight of the residues divided by

the weight of the dry sample multiplied by 100 and expressed as g/100 g of the dry weight sample. The ash content was determined by charring 2 g of pomace for 30 min, followed by incineration in a muffle furnace at 525 ◦C for 4 h, according to the AOAC Method 930.05. The residues obtained after incineration were recorded and divided by the weight of the sample weight and multiplied by 100 and expressed as g/100 g of the dry weight sample. The total carbohydrate content was calculated by subtracting the value of the protein, ash, and lipid contents from 100% of the dry weight. The soluble and insoluble dietary fiber were quantified using a Megazyme kit, based on the American Association of Cereal Chemists (AACC) Method 32-07.01 and the AOAC Method 991.43 [13]. One g of pomace (duplicate) was mixed with 40 mL MES-Tris buffer (0.05 M pH 8.2) and hydrolyzed with 50 μL of α-amylase (Megazyme E-BLAAM) at 95 ◦C for 30 min under constant stirring (120 rpm). After hydrolysis, the temperature was cooled to 60 ◦C and the sample was hydrolyzed with 100 μL of protease (Megazyme E-BSPRT) at 60 ◦C for 30 min under constant stirring (120 rpm). Then, the pH was adjusted to 4.1–4.8 with 0.561 N HCl and further hydrolysis was performed with 200 μL of amyloglucosidase (Megazyme E-AMGDF) at 60 ◦C for 30 min under constant stirring (120 rpm). The suspension was vacuum-filtered in the Fibertec 1023 E equipment (Foss System, Hilleroed, Denmark) through a celite (Megazyme cat. No. G-CELITE) in a bed crucible. The residues were washed with hot distilled water (70 ◦C), 95% ethanol and acetone, dried and recorded as IDF. The obtained supernatant was mixed with four volumes of 95% ethanol (60 ◦C) and left to stand at room temperature for 1 h; the SDF was recorded by filtration of the ethanolic suspension in the same conditions as the IDF and washed with 78% ethanol, 95% ethanol, and acetone. The IDF and SDF were calculated by subtracting the protein and ash contents determined in the obtained residues and expressed as g/100 g of the dry weight sample.
