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Materials and methods 99

Dalam dokumen 1. Title of the manuscript: (Halaman 36-39)

STARCHES WITH DIFFERENT DEGREE OF SUBSTITUTION

2. Materials and methods 99

2.1. Materials 100

Arenga starch (Arenga pinnata Merr.) 101

used for this study was obtained from Sigi 102

distric Central Sulawesi Province, Indonesia.

103

High-purity acetic anhydride 98%, sodium 104

hydroxide (NaOH) and hydrochloric acid 105

(HCl)were purchased from Merck. The 106

chemicals for analysis used in the study were 107

of analytical grade purchased at local agent.

108

2.2. Preparation of acetylated arenga starch 109

The acetylated arenga starches (AAS) 110

was prepared by a modified procedure of 111

Phillips et al. (1999) with modification. The 112

DS was determined by a titration method.

113

Starch (100 g) was dispersed in 225 mL of 114

distilled water and stirred for 60 min at 25oC.

115

The suspension was adjusted and controlled at 116

pH 8.0 ± 8.2 with 3.0% NaOH solution.

117

Acetic anhydride of (5, 10, 15 % starch base, 118

sb) was slowly added drop-wise to the stirred 119

slurry. After the complete addition of the 120

3 acetic anhydride, the reaction was continued 121

for 60 min and interrupted, setting the pH at 122

4.5 with 0.5 N HCl. The suspension was 123

precipitated for 10 min and subjected to two 124

successive washes twice with distilled water 125

and once with 95% ethanol, and then oven- 126

dried at 40oC for 48 h or up to approximately 127

12% moisture, and ground on an analytical 128

mill. Acetylation of starch with 5% (sb) acetic 129

anhydride gave the AAS with DS 0.039, with 130

10% (sb) acetic anhydride gave that with DS 131

0.078, and with 15% (sb) acetic anhydride 132

gave that with DS 0.139.

133

2.3. Determination of resistant starch 134

The RS determined as a dietary fiber 135

according to the enzymatic gravimetric 136

method (Ebihara et al., 2006). To determine 137

the content of RS, 4 g of sample was 138

suspended in 160 mL of 0.08 M phosphate 139

buffer (pH 5.5) before the addition of 40 µl of 140

heat-stable α-amylase. The solution was 141

incubated at 95°C for 75 min and then allowed 142

to cool. The pH of the solution was adjusted to 143

4.5 by adding 1 N HCl, and the sample was 144

incubated with amyloglucosidase at 60°C for 145

45 min. Aliquot (100 µl) was added with 10 146

mL of glucose oxidase reagent and the 147

mixture was incubated at 20°C for 20 min.

148

Absorbance was measured using a 149

spectrophotometer at 510 nm. The 150

concentration of RS was calculated as follow:

151

RS (g/100 g) = (1 – G × 0.9 / wt. sample) × 152

100, where wt. sample was the initial weight 153

(g), and G is the weight of glucose (g).

154

2.4. The bile acids/salts binding 155

The binding of bile acid/salts (cholic acid, 156

sodium taurocholic sodium deoxycholic) was 157

measured by in vitro analysis (Smietana et al., 158

2000). The sample (100 mg) was admixed 159

with 10 mL of solution of each bile acid. The 160

solutions were prepared in 0.1 mol phosphate 161

buffer pH 7.6for each bile acid in 2 µmol/mL 162

concentration. The samples and parallel blank 163

samples were incubated at 37°C for 30 min.

164

Centrifugation was performed at 2000 g for 165

5min. The sample (50 µl) was combined with 166

5 mL 70% sulphuric acid and 1 mL of freshly 167

prepared furfural solution (2.3 g/L) with 168

careful mixing of the whole sample.

169

Absorbance was measured at 510 nm after 80 170

min. The results were expressed as percent of 171

bile acid absorption.

172

2.5. The cholesterol binding 173

The cholesterol binding was measured by 174

in vitro analysis (Smietana et al., 2000). The 175

sample (100 mg) was combined with 2 mL 176

emulsion composed of 1% lecithin, 1.375%

177

sodium salt of deoxycholic acid and 0.225%

178

cholesterol prepared in 0.1 mol phosphate 179

buffer of pH 6.8. Incubation for 1 h at 37°C 180

was performed in a shaking water bath.

181

Cholesterol absorption by 20 µl emulsion was 182

analysed using reagent kits. The results were 183

expressed as percent of cholesterol adsorbed 184

by samples.

185

2.6. Preparation and operation of batch 186

fermenters 187

Fresh faecal samples from a healthy 188

human volunteer who had no history of 189

antibiotics treatment in the previous 3 months 190

were first diluted (1:10) in anaerobic buffer 191

containing 0.1 M phosphate-buffered saline 192

(PBS) solution, pH 7.0, and then were 193

homogenized using a magnetic stirrer at 194

normal speed for 2 min. A 10 mL portion of 195

the filtered faecal slurry was added to 90 mL 196

growth medium in 250 mL batch fermentation 197

vessels. The growth medium contained the 198

following ingredients: peptone water (2 g/L), 199

yeast extract (2 g/L), NaCl (0.1 g/L), K2HPO4

200

(0.04 g/L), KH2PO4 (0.04 g/L), MgSO4.7H2O 201

(0.01 g/L), CaCl2.6H2O (0.01 g/L), NaHCO3

202

(2 g/L), Tween 80 (2 mL/L), Hemin (0.05 203

g/L), Vitamin K (10 µL/L), L-cysteine (0.5 204

g/L) and bile salts (0.5 g/L). The NAS and 205

BAS (1% w/v) were added to each vessel just 206

before addition of fecal slurry (10% w/v). The 207

vessels were maintained under anaerobic 208

4 conditions by continuous sparging with 209

oxygen-free nitrogen. Temperature was 210

automatically controlled at 37 °C. The batch 211

experiments were performed in duplicate with 212

two different fecal donors for each substrate.

213

At each experiment a 5 mL sample was taken 214

from each vessel at 0, 12, 24, and 48 h for 215

analysis (Vardakou et al., 2008; Ramnani et 216

al., 2012).

217

2.7. Bacterial enumeration 218

The samples from each vessel were 219

immediately transferred to an anaerobic 220

cabinet containing an atmosphere of 10% H2, 221

10% CO2, and 80% N2, and were serially 222

diluted with pre-reduced half strength peptone 223

water, pH 7, supplemented with 0.5 g 224

cysteine–HCl L-1. Portions of 1 mL from each 225

dilution were plated, in duplicate, onto agar 226

plates (incubation anaerobic condition at 37oC 227

for 48 h). The selective growth media used 228

were total plate count, for total bacterials;

229

trypticase soy agar, supplemented per litre 230

with 75 mg kanamycin, 5 mg haemin, 75 mg 231

vancomycin and 50 mL laked horse blood, for 232

Bacteroides spp.; reinforced clostridial agar, 233

supplemented per litre with 8 mg novobiocin 234

and 8 mg colistin, for Clostridium spp.; rogosa 235

agar, supplemented with 1.32 mL glacial 236

acetic acid L-1, for Lactobacillus spp.;

237

Columbia agar containing per litre 5 g 238

glucose, 0.5 g cysteine HCl, and 0.5 mL 239

propionic acid, pH 5.0, for Bifidobacterium 240

spp. All agars were purchased from Oxoid 241

(Basingstoke, Hants, UK) and prepared 242

according to the supplier's instructions. All the 243

antibiotics used in the preparation of media 244

were purchased from Sigma.

245

2.8. Calculation of prebiotic index 246

The equation used to estimate the 247

prebiotic index (PI) values (Palframan et al., 248

2003) was:

249

PI = (Bif /Total) – (Bac / Total) + (Lac / 250

Total) – (Clos /Total) 251

where Bif, Bac, Lac, Clos, and Total are the 252

numbers of bifidobacteria, bacteroides, 253

lactobacilli, clostridia, and total numbers of 254

bacteria, respectively, at the time of sampling 255

relative to their respective numbers at the time 256

of inoculation. The equation embodies the 257

assumption that an increase in the populations 258

of bifidobacteria and/or lactobacilli is a 259

positive effect while an increase in bacteroides 260

and/or clostridia is a negative effect.

261

2.9. Determination of pH 262

The pH of the samples was determined 263

using a digital pH metre (Eutech instruments, 264

Cyber scan) calibrated with buffers at pH 4.0 265

and 7.0 (Fisher Scientific, UK).

266

2.10. Determination of organic acid 267

Culture medium (1 mL) was centrifuged 268

at 4500 x g for 30 min. The supernatant was 269

filtered through a 0.22 mm filter into a 1.5 mL 270

eppendorf tube for storage at 4oC until use.

271

Samples of 1 µL were injected into a high- 272

resolution gas chromatography (GC Shimadzu 273

8A) equipped with a flame ionization detector 274

and an HP Innowax 19091 - 136 column (GP 275

10%-SP 1200/1% H3PO4 on 80/100 mesh 276

chromosorb WAW, 60m x 0.250 mm). The 277

carrier gas was nitrogen with a flow rate of 1.8 278

mL/min, and the split ratio was 40:1. The 279

oven temperature was maintained at 90oC for 280

0.5 min, and then increased to 110oC at a rate 281

of 10oC/min, increased to 170oC at a rate of 282

5oC/min and finally increased to 210oC at a 283

rate of 20oC. Injector and detector 284

temperatures were 230oC. SCFA mixture 285

containing acetate, propionate and butyrate at 286

specific concentration were used as standard.

287

2.11. Statistical analysis 288

The data experiments were analyzed 289

using SPSS (version 17.0) software and 290

subjected to one-way analysis variance. The 291

5 difference of means between groups was also 292

analyzed using Duncan’s multiple comparison 293

test. The level of P < 0.05 was considered as 294

significant. All experiments were repeated 295

once or twice at later dates.

296

3. Results and discussions

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