Effect of Silkpeptide on Physicochemical Properties of Bread Dough

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(1)KOREAN J. FOOD SCI. TECHNOL. Vol. 36, No. 2, pp. 246~254 (2004). ©The Korean Society of Food Science and Technology. \Ï Î& >#~ z ßW B ^* B* ^zBB. Effect of Silkpeptide on Physicochemical Properties of Bread Dough Young-Ho Kim* Department of Hotel Baking Technology, Hyejeon College Physicochemical properties of bread dough added with silkpeptide were investigated. Protein content of silkpeptide was 90.83%. In amino acid analysis, glycine content was highest at 18,760.04 mg%. Alanine, serine, and tyrosine contents were much higher in silkpeptide flour than wheat flour. Mixed silkpeptide showed low lightness and redness values and high yellowness. Farinograph water absorption decreased as silkpeptide content increased. Both arrival and development times of silkpeptide-added dough were longer than those of wheat flour. As silkpeptide content increased, degree of weakness increased. Maximum viscosity of amylograph decreased gradually with addition of silkpeptide, while gelatinization temperature was not affected. Extensograph showed extensibility and resistance to extension of dough increased, while ratio of resistence to extensibility highly increased with increasing amount of silkpeptide. Silkpeptide added to bread dough showed oxidation effect, indication that it could be used as natural additive for improving bread dough quality. Key words: bread dough, silkpeptide, farinograph, amylograph, extensograph. B. . V ÒW Ï& W>º ©b rJ^ ® (5). Luo (6)f rat~ þöB b2 R .~ çß ÛB>îb, .Ó .Êr ³ê~ &~& &V>î ~& . Keiko (7)f 6% Ï Ïj Î&~ B &f zæ Î"& Ö>~ ~& . b 2~ &¦ªj Næ~ ®º glycine, alanine, serine 5 tyrosine jÖf ~£® 5 VËW ®bB~ Ïö & & ê¯> ®Ú ¢ Ï îÚ ²Ò~ ª¢& F © . æ.ræ B α-glucosidase ÛB·Ïö ~ .; ~VË, .Ó .Êr" 7Wæî 6²VË, zæ VË 5 ÷ ~ò VËj &ê Ï¢ ~ ²Ò Ï b ÒW Î"¢ æò VËW ~ B VF j BB~º ©f î÷~ ~ò¾ .Oj *~ jº~ '>î . º Ï Î&ïj Ò~ >#~ bW ßW j «b Ï Î& B >#~ >N, b W, êKW, BÎÚK B ;öB jº ~º B> ¶ò¢ ªC Òb ®î ßW" & Ö> Ï Î&ö & "' BO»j »~º ¶ò B Ï~¶ ~, Ëê Ï ÒÏ~º wÏº*¢ {&~ j j "¶~f · ®& BÖëö. Ï¢ Î& B®BBj ÖëÚö ²B~ ¢ Ï > ®º 2/ Î"ö 'Ë ©b 6B . V¢B öBº VËW ®²Ò Ï¢ Bö Î. ·ÆÖb (silk)º " ®²ÒB z' W C &æB VËW ® ²Ò BB > ® . b2 f Â WîB Bê& ¸bBê ï Ö &Ë j Ö ¶öb(1) ^Ò" b2b W>Ú ®b & >ªÊ FÒjÖ" oligopeptide~ ; Ï & B (2). Ïº >ÏW ;B Î j>j Ö F>Ú ®b 18&æ~ jÖj F~ ® .. b2~ jÖ 7 glycinef rat~ þöB .Ó . Êr çßj ÛB~º Î"& ®b(3) alaninef r&Ò ¢ /êB ?f rö ~ *Ë¢ .O~ tyrosinef ~ Ãj .O~¾ ~ò~º £Ò' VË ®º Væ j Ö ³¦~ ^Ò 5 ¶Ö ªjö 'Ëj ~ º ©b rJ^ ® (4). ®öB Ïº '·, Ò ;VËWö 'Ëj b ®ö Ö 7º j . ¢>'b Úöº ; ÒWj <º FÒÏ & ô ®b, ®öº «~~ Ï BÎ ~ &¾Ò 7ö ^ > ®b 7öº ® Wî¦ *Corresponding author : Young-Ho Kim, Dept. of Hotel Baking Technology, Hyejeon College, Namjang-ri, Hongsung-eup, Chungnam 350-702, Korea Tel: 82-41-630-5239 Fax: 82-41-631-4405 E-mail: [email protected] 246.

(2) Ï Î& >#~ z' ßW. &~&j r >#~ z' bWßWö ~º 'Ë j Ò~ Ï Î&~ BO»j {ã~¶ .. Òò 5 O» Òò þö ÒÏ &&º (")&Bª ;Kª, Ï º (")z:Ò B®j ÒÏ~&b, ># VjöB. Ï Î&ïf Æ ¢bÞ(baker’s percent) && 100% V&ö & 0, 0.5, 1, 2, 3 5 4% '' Ò~ Î &~& . ¢>Wª. Ïf &&~ ¢>Wªf AOACO»(8)ö V¢ ª C~& . ¯ >ª ïf 105oC~ ç{ &», ²ªf 600oC~ ç7²z», Wî ïf micro-Kjeldahl »j Ò Ï~&, æO ïf Soxhlet ºÂ»b G;~& . R Fº Prosky (9)~ O»b total dietary fiber G;Ï(Sigma Co., MO, St. Louis, USA)£j ÒÏ~ G;~& . jÖ. Ïf &&~ jÖ ªCf Bidlingmeyer (10) ~ O»ö ~ ¢;ï~ ò¢ 6 N-HCl Ïf b~ î ² Ïê ê 110oCöB 24* ÿn &>ª ê 50 mL ; Ï~& . ¢ 0.45 µm membrane filter "~ 20 µL¢ ~ ê ~& . B òö methanol : water : triethylamine (2 : 2 : 1) Ï 30 µL¢ Î&~ 2N ê Vö Fê Ú £ methanol : triethylamine : H2O : phenyl isothiocyanate = 7 : 1 : 1 : 1, V/V)j 30 µL &~ 20ª* O~ ê 3N ~ & . methanol 30 µL¢ Î&~ ~ sodium acetate buffer(pH 6.4) ÒÏ~& . ¢ HPLC(High performance liquid chromatography, Waters Associates Inc., USA)¢ ÒÏ~ Table 1~ öB ªC~& . FÒjÖf ò 2 gj ï~ 200 mL~ 80% ethanol 80 µLöB 6* ~~ ºÂ ê "~ 6{ Ê .B>¢ Î&~ 20 mL ;Ï~ ò ºÂb ~& . ò ºÂj jÖ ª CÏ lithium citrate buffer 20V C r 0.45 µm membrane filter "~& . FÒjÖf HPLC¢ ÒÏ~ Table 1~ b ªC~& . Z8î. Ïf &&~ ZVî ªCf ²z»b ~&. . ¯ ò¢ 550oCöB 4* ÿn ²zÎ ê 0.2 N HNO3 Ïö Ï~ 100 mL ;Ï ê "~& . ªCf ICP (Inductively coupled plasma, Jobin-Yvon Model JY 38 Plus, France)¢ ÒÏ~ Table 2f ?f b ~& . FÒ. Ïf &&~ FÒ ªCf ò 2 gj ï~ 200 mL~ 80% ethanol 80oCöB 6* ~~ ºÂ ê " ~& . ¢ 6{ Ê .B>¢ Î&~ 20 mL ; Ï~ ò ºÂb ~& . ò ºÂ 0.2 mL¢ î²V ~~ö j*® Î ê pyridine 1 mL¢ &~ &N~ B .r2 j*® hexamethyldisilazane 0.2 mLf trimethylchlorosilane 0.1 mL¢ &~ >wÎ ê GCö "«~. 247. Table 1. Operating conditions for analysis of amino acid by HPLC UV/VIS detector 254 nm Column: Water pico-tag column (3.9Ü150 mm, 4 µm) Column Temp.: 40oC Mobile phase Eluent A: 0.14M sodium acetate trihydrate 0.05% trithylamine (pH 6.4 with phosphoric acid) Eluent B: 60% acetonitrile Table 2. Operating conditions for analysis of mineral by ICP Nebulizer pressure Aerosol flow rate. 3.5 bar for Meinhard type C 0.3 L/min 0.3 L/min for multielement analysis of aqueous solutions 12 L/min. Auxiliary gas Cooling gas. Table 3. Operating conditions for analysis of free sugar by GC Insrument: HP-5890 series II plus with HP-6890 Autoinjector Detector: FID Column: HP-5 (30 mÜ0.25 mmID) Injector Temp.: 250oC Detector Temp.: 280oC Column Temp.: 150oC (0 min)-10/min-250 (5 min)-20/min-280 (7) Carrier gas: N2 1 mL/min. Table 3~ b ªC~& . «¶~ \8. Ïf &&~ «ê ªº LS particle size analyzer (Coulter LS 100, USA)¢ Ï~& . ªÖj * Ï º isopropyl alcoholj ÒÏ~& ¦b(%)ö & «¶çãb G;® . ¦b¢ 100% ~ 40 µmöB 900 µmræ~ «¶ çãj G;~ «ê~ ï8, n~ 5 C 'j êÖ ~& . ïN. Ïf &&~ ïNº ïêê(Color and color difference meter, TC-3600, Japan)¢ Ï~ G;~& . Ï º VjNö V¢ BV(Hobart kichenaide K45 10-speed mixer) 5ª* b ê ïN¢ G;~ Hunter systemö ~ ~ «ê(L, lightness), 'ïê(a, redness), ïê(b, yellowness) 8b ¾æÚî . L8f 0(¦;ï)öB 100(ï)ræ, a8('ïê)f −80(ï)öB 100('ï)ræ, b8(ïê)f −70( Óï)öB 70(ï)ræ G;~& . &6f Wï6j ÒÏ~ & Wï6 ¾æÚº L, a, bº '' 89.2, 0.923, 0.783 î . Hunter scaleö ~ CïN(∆E, total color difference) º G;B L, a, b 8j Ï~ r" ? êÖ~& . ∆E =. 2. 2. ∆L + ∆a + ∆b. 2. pH ># 5 ò&~ pH G;f ò 10 gj '' 250 mL j ö I 100 mL Ã~>¢ & r ¢~² b~ 25oCöB 30ª* O~ ê çj pH VV G;~& ..

(3) ®"²æ B 36 ² B 2 ^ (2004). 248. \Ï~ ª¶ï Sephadex G-50(Pharmacia Biotech., Ltd., Uppsala, Sweden) column chromatography¢ ÒÏ~& . 0.01 M buffer(0.01 M sodium phosphate, 0.15 M NaCl, pH 7.2) Ò >zÎ Sephadex G-50 reginj îV~ j* >zÎ ê 1.2 cmÜ30 cm glass columnö ÏêB n;zÎ . Ò silk protein hydrolysate¢ buffer 1 mg/mL>² B Ïj Vö 200 µL Î&~& . ê fraction collector(Pharmacia Biotech., Sweden)ö 2 mLO Ïj ê 280 nm~ 2ËöB 7ê ¢ G;~ chromatogramj jW~& . ª¶ï {j * gel filtration prestained molecular standard(Bio-Rad Lab., Hercules CA, USA)¢ ÒÏ~& . &bî f thyroglobulin(670 KDa), bovine gamma globulin(158 KDa), ovalbumin(44 KDa), myoglobin(17 KDa), vitamin B-12(1.35 KDa)¢ ÒÏ~& . VB standard chromatogram" ò~ chromatogramj jv~ silk protein hydrolysate~ ª¶ïj ~& .. extensograph(Brabender Co., German) rounderöB 20® ;ê &ÒV¢ ~ öÛ;b W;~& . ¢ 30Û2oC~ BÎ öB 45, 90 5 135ª* BÎÎ ê ' *î >#~ Ëê, &ê 5 *Ú'j G;~& . Ëê(E)º ·6b ¦V ræ~ Ò(mm), &ê(R)º ¾*~ ¸ (B.U.) ¾æÚ jNf R/E ¾æÚî .. Ö 5 V ¢>Wª þö ÒÏB Ïf &&~ ¢>Wªf Table 4f ? . Ï~ >ªf 5.80% Ô~, Wîf 90.83% ï ç® ¸f ßûj &b æO" R Fº '' 0.05%f 0.48% Ö Ô~ . &&º >ª ï 14.0%, Wî" ²ªf '' 12.46%, 0.413% ;K ªî . Ïº ®öB " > ìº Wîö $ oligopeptide W>Ú ®Ú VËW 5 '·' öB ®ö Ï &~& ¸ . V¢B Ï¢ ö Î&b VËW ® ²Ò wÏ BB > ® . Ïº 90%ç~ WîV r^ö Bö Ï ã Ö BÎ"; 7 jÏ·Ï Î" BÎ~ æ .G> ¢ ~V * ÖB~ Î& >#~ pH ;j J¢ F ©b 'B . &&f Ï~ pHº '' 5.80" 6.16 &&. Ï& ¸~ . ÊÞ~ BÎ ³ê º Î&B öò~ pHö 'Ëj Ab BöB pHº 7º j ~º ©b rJ^ ® (14).. .^\` ªC. Ïf && 5 >#~ .^º "Ò*¶ * ãb &V~& . ò>#f b êf 2N BÎ ê ª ~ ÿÖ B ÒÏ~& . ò(40Ü40Ü30 mm)¢ r ª ææ& *ö ß, JEOLN ê.V(JFC-1100, Japan)¢ Ï~ .;b ÞÖ, JEOLÒ(JSM-35F, Japan)~ "Ò*¶*ãj Ï~ &³*{ 15 KVöB R'~& . Farinograph AACCO»(11)ö V¢ farinograph(Brabender Co., German)¢ Ï~& . Farinograph mixing bowlj 30Û0.2oC Fæ~ê ~& . òº >ªï 14.0% V&b 300 gj ÒÏ~& , F~ 7F 500 B.U.(Brabender Unit)ö ê~ê Ã ~>¢ &~& . Ò >N, >#ê*, >#;W*, n;ê 5 £zê j G;~& .. jÖ. Ïf &&~ jÖ Wf Table 5f ? . & &~ CjÖf 7549.76 mg%& . *Ú'b glutamic acidf proline~ ïf '' 3443.00 mg%f 794.13 mg% ¸ ~b lysine, methionine, tyrosine 5 cystine ~ ïf Ô² ¾æÒ . º Kim (15)~ &&~ jÖ Wö & f FÒ~& . Ï~ CjÖf 50224.12 mg% &&~ CjÖ 6.7V Ö ¸f ïj ¾æÚ î . jÖ Wf glycine(37.4%)~ ï B¢ ô~b alanine(28.2%), serine(14.7%) 5 tyrosine(8.6%) Bb ¾æÒ C ïf *Ú jÖ ï~ 89% ¸f jNj Næ~& . º Nahm (16) jÖ W" F Ò~& . Ï¢ ö Î&b Wî ;zf. · jÖj ; > ®º '·' 5 Ò' W~ Î"& çú~ VËW ® ²ÒB Ï&~& Ö ¸f ©b 'B .. Amylograph AACCO»(12)ö V¢ amylograph(Brabender Co., German)¢ ÒÏ~ ªC~& . ò 65 g(>ª 14%V&)ö Ã~> 450 mL¢ Î& ê *çb ~ ÒÏ~& . 25oC¦V 95oCræ 1.5oC/min ßNÊB 6êæz¢ G;~& . G ;BNêº 25oC¦V ·~ ^zBNê, 6êNê 5 6ê~ ßW8j G;~& . ^zB Nêº .V6 ê& 10 B.U.ö ê~º Nê ¾æÚî . Extensograph AACCO»(13)ö V¢ ò 300 g(>ª 14%V&)j farinograph bVö I farinograph~ >N 2-5%~ 'f · ~ Ã~>ö ². 2%(6 g)¢ ÏÎ Ïj ÒÏ~& . 1ª * b r 5ª* O~~ >#j ·~ farinograph~ 500 B.U.ö F~ 7 ê~ê jºö V¢ >ïj .~& . ># Â r 150 g(2B)~ >#j. Z8î. Ïf &&~ ZVî ïf Table 6" ? . Ïº îJ¾~ ï 702.35 mg% B¢ ¸~b. rb ¢¾, 5 ¾Þ Bb ¸~ ¢, Æª ZV"~º Ô~ . B Ï Î&º &&ö ¦. Table 4. Compositions of wheat flour and silkpeptide. Wheat flour Silkpeptide. Moisture (%). Ash (%). Crude protein (%). Crude fat (%). Crude fiber (%). pH. 14.0 5.80. 0.413 1.985. 12.46 90.83. 1.23 0.05. 0.14 0.48. 5.80 6.16.

(4) Ï Î& >#~ z' ßW Table 5. Total amino acid compositions of silkpeptide and wheat flour (mg%) Amino acids Aspartic acid Threonine Serine Glutamic acid Proline Glycine Alanine Cystine Valine Methionine Isoleucine Leucine Tyrosine Phenylalanine Histidine Lysine Arginine Total. Wheat flour. Silkpeptide. 272.53 177.88 342.29 3443.00 794.13 241.02 177.19 94.42 269.73 72.08 231.53 475.09 93.35 351.26 154.44 156.53 203.29. 728.69 523.87 7367.23 919.91 246.12 18760.04 14173.40 90.10 1096.82 80.50 320.11 276.67 4213.76 404.74 439.01 287.60 295.55. 7549.76. 50224.12. Table 7. Free sugar content of silkpeptide and wheat flour (mg%). Wheat flour Silkpeptide. ZVî~ Ïö~ êæ F > ®rj & . &&º 85.63 mg% B¢ ¸~ Æ, j 5 *f ç&'b 'f ª¢ ¾æÚî . ï ôf f ~ 7ö >Ú ®º phytate~ ï" ¸f ç& &ê¢ < ®b & ~ óî¦ªö ô F>Ú ® . &&º &ö j ZV î ï ç '² F>Ú ®º, º &¦ª~ ZV î bf ^ª[ö Ò~ ®Ú Bª çï ¶ > V r^ . FÒ. Ïf &&~ FÒf Table 7" ? . &&~ FÒf sucrose& 117.35 mg% B¢ ô~ fructoseº 7.65 mg% Ô² ¾æÒ . &&ö FB f BÎB®ö B ÎW b B>æ Bö ®ÚB 7º j . Þ Ï~ FÒ 7 fructoseº 9.35 mg%, maltose 5.30 mg% Ò glucose 2.10 mg% *>'b ï Ô ² ¾æÒ . «¶\8, ïN 5 \Ï~ ª¶ï. Ïf &&~ «¶ Vº ªêº Fig. 1" ? . ï«¶ Vº &&& 66.95 µm, Ï& 15.95 µm. . * ¦b 'f &&& 4041 cm2/mL, Ï º 9976 cm/mL ¾æ¾ &&. Ï~ «¶& z ^~&b &&º ·f «¶f «¶ ªÖ>Ú ® «¶f 50-150 µm *Ú'b ôf ¦ªj Næ~ ®b ·f «¶ f «¶ 'f ·b 1-10 µm " 20-50 µm b ªÖ>Ú ®î . º Kwon(17) . 249. Sucrose. Maltose. Glucose. Fructose. 117.35 1.73. 36.39 5.30. 28.54 2.10. 7.65 9.35. Fig. 1. Particle size distributions of wheat flour (A) and silkpeptide (B).. ;Kª~ «¶ ªf FÒ~& . &&~ «¶Vº ïç" >z³êö 'Ëj "Ú ^> ïj >z ³ê& ¢ê . Þ Ï~ «¶ªêº &&f jÝ ;¢ &b¾ «¶º && ·f 12-35 µm ;ê~ j ;W~& . &&ö Ï~ Î&ïj Ò~ b &~ ï Nº Table 8" ? . L8~ ãÖ && 100% &º 92.46& Ï Î&ïj 2.0%, 3.0% 5 4.0% Ã& '' 91.84, 91.47 5 91.25 8 .O Ôjr . 'ï ê¢ ¾æÚº a8öB &º −0.93îb¾ Ï¢ 2.0%, 4.0% Î& ãÖ '' −1.23, -1.44 r~ 8 ² ¸jr . b8f && 9.05, Ï¢ 2.0%, 4.0% Ã & ãÖ '' 11.03, 12.82 8 £*O ¸jr, Cï N ∆E8f Ã&~ Ï Ã& £*~ ÚvÚ ïj ¾æÚî . Þ Ï~ ª¶ïf Fig. 2f ? 15001600 Dab G;>î .. Table 6. Mineral compositions of silkpeptide and wheat flour. Wheat flour Silkpeptide. (mg%). K. Na. Ca. Mg. P. Fe. Mn. Cu. Zn. 40.52 23.24. 12.27 97.65. 20.36 201.35. 5.15 702.35. 85.63 156.25. 0.4753 41.25. 0.3765 0.1423. 0.0432 0.6784. 0.0324 0.8652.

(5) ®"²æ B 36 ² B 2 ^ (2004). 250. Table 8. Color values of flour blended added with silkpeptide Silkpeptide (%) 1). L a2) b3) ∆E4). 0. 0.5. 1.0. 2.0. 3.0. 4.0. 92.46 -0.93 9.05 0.00. 92.29 -0.96 9.48 0.44. 92.19 -1.00 9.69 0.68. 91.84 -1.23 11.03 2.09. 91.47 -1.31 11.90 3.03. 91.25 -1.44 12.82 3.99. 1). L: Degree of lightness (white 1000 black). a: Degree of redness (red +100-80 green). 3) b: Degree of yellowness (yellow +70-80 blue). 2). 4). ∆E =. 2. 2. 2. ∆L + ∆a + ∆b (total color difference).. Fig. 2. Determination of molecular weight of silkpeptide by gel permeation chromatograph using Sephadex G-50.. .^\` ªC. Ïf && 5 >#~ .^¢ "Ò*¶* ãb &V Ö"º Fig. 3" ?~ . &&º *ª «¶. " Î·~ ; &V>îb *ª«¶º 5-20 µm~. · V ª>Ú ®î . Wîf *ª «¶¢ ® bB f B oöê ÚÒ¢ ;W~& .. Ïº ~ ö;ö &rÖ ö Ú¦ Ö>Ú ®º Î·j j ·f " s ô J^ ®î . «¶Vº 10-45 µm «¶& ·~&, «¶. z ªB ©b º ·f ' ª>Ú ®î. . f ? «¶ ö J ®º ·f s f. Ï~ ÏWj £² ~ ; >W~ ßWj ¾æÚ º ©b º;B .. Ï¢ Î& >#~ .^º Fig. 4f ? . b ê >#~ .^¢ &º *Ú'b proteinstarch matrix ;W>Ú ·f ;~ *ª «¶& ® 'b &ê ®² ¾ ª>Ú ® j# } ç& . *ª «¶~ Vº © çã 15-25 µm ; ê ·f *ª «¶º 2-10 µm ;ê V& ·~& . º Parades (18) ¾ ;WB && >#" FÒ Î·î . Parkkonen (19)f '.~² bB >#~ & vf f ïb ;W>Ú *ª¾ ¦Òò R >Ú ªÖ>Ú ®b BÎ& ê¯Nö V¢ >#ö V ; WB ~& . þ~ ^ &VöBê &~ ã. Fig. 3. Scanning electron micrograph (Ü1,000) of wheat flour and silkpeptide.. Ö &v matrixö *ª ªÖ>Ú ®º ©j &V > ® î, BÎ ê .^º BÎ ÿnö protein-starch matrix ~ & £* Þ^ & . Ò &Ê Bb V æB *ª «¶¢ ®~ Wî~ ï ½Î ^ ®º © &V>î . Protein matrix Ú¦öº ·f V ¾æÒb $ *ª «¶ 7 ¢¦& ª>Ú . ¾ ² æ;B Î·b .¢^ ¶çj «f © & V>î .. Ï¢ 1.0% Î& >#~ .^º &f ? f n;B ¢ &b¾ 3.0% Î& protein-starch matrix º &ö j ®n;~² £V ê~ ~ ¦b.

(6) Ï Î& >#~ z' ßW. 251. Fig. 5. Farinograms of wheat flour added with various levels of silkpeptide (SP).. Fig. 4. Scanning electron micrograph (Ü1,500) of fresh mixed dough and fermented dough added with silkpeptide. (A) Fresh mixed dough of 100% wheat flour (B) Fermented dough of 100% wheat flour (C) Fresh mixed dough with 1.0% silkpeptide (D) Fermented dough with 1.0% silkpeptide (E) Fresh mixed dough with 3.0% silkpeptide (F) Fermented dough with 3.0% silkpeptide.. 5 ®î~ çº ² &~N .G>î . Pomeranz (20) f && ># öB *ª «¶º z× æ ·f « ¶º £* æ;>B protein matrixf Ö~º ·çj & b, º protein-starch ç^·Ï ;z>º ©b BÎf z®Ú ^ b öB êKW ®² æz~ ·f n *j ;W~ Wîf *ª «¶¢ ® ~& . Farinograph. Ï Î&ïö V farinogram ßWf Fig. 5, ßW8. f Table 9f ? . & &&~ >Nf 63.1%& .. Ï0.5%, 1.0%¢ Î& >Nf 63.1%f 62.1%& 3.0%, 4.0%öBº '' 60.4%f 59.3% Ï& Ã& > >Nf 6²~º ãËj ¾æÚî . >#~ >z³ê¢ ¾æÚº >#ê*f Ï 1.0% Î& 1.8ªî . Î&ïj Ã& 3.0%, 4.0%º '' 2.0 ª, 2.7ªb &~ 1.5ªö j * ² Ë>î . >#~ V& ö ê~º >#;W*f 1.0% Î& 6.0ªb &~ 5.0ª" £*~ N¢ &b¾ 3.0%, 4.0% Ã& '' 7.0ª, 7.5ªb ^Úr . n;êº && 15ªî . Ï 2.0% Î&ræº &f jÝ n ;ê¢ &b¾ 3.0%, 4.0% Ã&º '' 13ª" 11.5ª b Ï~ Ã&ö V¢ n;êº Ô~ . £zêº & & 40 B.U.&b¾ 1.0%º 50 B.U. £* Ã&~& . Î &ïj Ã&Î 3.0%, 4.0%º '' 65 B.U.f 75 B.U.. Ï& Ã&> >#~ £zê& æº *çj &. . >ª >Nf farinographö ~~ Ö;B . && >. Table 9. Farinogram characteristics of wheat flour added with various levels of silkpeptide Silkpeptide (%) Water absorption (%) Arrival time (min) Development time (min) Stability (min) Weakness (B.U.). 0. 0.5. 1.0. 2.0. 3.0. 4.0. 63.1 1.5 5.0 15 40. 63.1 1.7 5.0 16 40. 62.1 1.8 6.0 16 50. 61.0 1.5 6.5 15 55. 60.4 2.0 7.0 13 65. 59.3 2.7 7.5 11.5 75.

(7) ®"²æ B 36 ² B 2 ^ (2004). 252. Table 10. Amylogram characteristics of wheat flour added with various levels of silkpeptide Silkpeptide (%) o. Starting temperature ( C) Gelatinization temperature (oC) Temperature at max. viscosity (oC) Max. viscosity (B.U.). 0. 0.5. 1.0. 2.0. 3.0. 4.0. 25.0 59.5 90.0 780.00. 25.0 59.5 90.5 770.00. 25.0 59.5 90.5 720.00. 25.0 59.5 90.5 720.00. 25.0 59.5 90.5 690.00. 25.0 58.0 90.0 645.00. Fig. 6. Amylograms of wheat flour added with various levels of silkpeptide (SP).. Nö 'Ëj "º º²º Wî ï" *ª ß® ¶ç*ª ~ ï 5 ÂÆÖ ï ö V¢ æzF > ® . þö B~ Ï Î&ö V¢ >ª>N 6²º Wî~ C Î" ê . Amylograph. Ï Î&ïö V amylogram ßWf Fig. 6, ßW8 f Table 10" ? . ^zBNêº 100% && &º 59.5oCîb Ï 3.0% Î&ræº &f ÿ¢~ &, 4.0% Î&º 58.0oC & Ô~ . 6êN êöB Ï Î&f &º N¢ æ p~ . 6êº && 780 B.U.&b¾ Ï¢ 2.0%, 4.0% Ã&º '' 720 B.U.f 645 B.U. 6²~º ãËî. . Amylogram~ 6êº Î²~ Wö *ª~ cJ ;ê ö ² 'Ëj Ab *ª «¶~ cJ ;êº *ç~ pH ¯ rÒWöB ² /êB (21). þöB 6ê~ &~ º α-amylase~ Wz~ Ö" º Ï Î&ö ~ *ª~ CÎ"ö &N ®º ©b 'B .. Extensograph. Ï Î&ïö V >#~ extensogramf Fig. 7, ß W8f Table 11" ? . Fig. 7~ & &&º &êf Ëê& ;j Ú &Ê FK ± BW ' j " *;' ;Kª~ Î·j & . & >#~ &êº 45ªö 560 B.U.öB 90ª ã" 620 B.U., 135ª ã " êöº 700 B.U. 8 * ã"ö V¢ Ã&~&. . Ëê~ 8f ¾r 45ªf 183 mm, 90ª, 135ª ã" 170 mm, 162 mm jr, resistance/extensibility(R/E) jº 45ª, 135ªræ *~ ã"ö V¢ '' 3.06, 4.32 Ã&~ & .. Ï Î&º BÎ* 45ª, 135ª ã"ö V¢ & êº Ã&~& Ëêº 6²~&b ö V¢ R/E j º Ã&~& . Ö"º && ># BÎö ~~ êW" 6W Ã&> Ëêº 6² º Hoseney (22) ~ f ¢~~& . Ï 0%öB 4.0%ræ Î&~& j r * ã"ö V¢ Ëê~ æz¢ 45ª ê & º 183 mm, 4.0% Î& 150 mm, 90ª êº && 170 mm, 4.0% Î& 110 mm, 135ª êº && 162 mmöB 4.0% Î& 85 mm BÎ* ã"f Ï Ã&ö V ¢ Ëêº 6²~& . &êº 45ª ê &º 560 B.U. &, 4.0%º 860 B.U.& . * ã" 90ª, 135ªöB & º 610 B.U., 700 B.U. ¾æÒ . &êº Ï 1.0% Î&º 90ª, 135ª ã" 900 B.U., 1000 B.U. &ê& Ã&~V ·~&, Ï 2.0% ç Î&º 90ª ê ¦V &ê& /Ï® Ã&~º ß *çj &b, 8f ¾*~ 6 1000 B.U. ¢ ² ½Ú¾ ;{ &ê 8j £j > ìî . *Ú' f 45ª ê &º 133 cm2îb¾ 2.0%º 170 cm2, 4.0% º 182 cm2 Ï Ã&ö V¢ ' ² Ã& ~ &, 2.0% ç Î&º 90ª ê¦V æ¾ &ê~ Ã& ¾*~ *Ú'j G; > ìî . Ö"º ¢ >'b ª j Î& bª~ ãÖ *Ú' 6²~ º ©"º >&~ *ç ¾æÒ . Ëêf &ê 8~ j N R/E8~ æzº Fig. 8" ? Ï Ã&ö V¢ * ã" R/E8f Ã&~&b, ß® 2.0% Î& 90ª ê¦Vº ² Ã&~ G;8j ¾æâ >& ìî . V¢B. Ï¢ Î&~º ãÖº >#~ &Ê FK" BÎ Ú K &&ò ÒÏ ãÖ º ² Ã&>Ú ÖzB¢ Î& ># bWj & . Cho (23)f >#ö ÖzB, ~ öB¢ Î&~&j r R/EjN Ã& BÎ*j »~&. ~& . ÖzB ascorbic acid, KBrO3 f Wî~ Ë W" &ÊF ËKj ;~ ~ & ¦b¢ á¶ ~ º ®, Wî~ -SHVö ·Ï~ -SHf -SS~ ç^v~ ·Ïj ÛBb BÎ"; 7 ËWj 6²Ê & ê~ Ã& R/E j¢ Ã&Êº ©b >Ú® (24)..

(8) Ï Î& >#~ z' ßW. 253. Table 11. Extensogram characteristics of dough added with silkpeptide after 45, 90, and 135 min rest time Silkpeptide (%) Rest time. 000. 00.5. 01.0. 02.0. 03.0. 04.0. 060. 59.8. 58.5. 57.9. 56.8. 56.0. Extension (mm). 45min 90min 135min. 183 170 162. 171 157 143. 169 150 127. 170 132 100. 147 114 92. 150 110 85. Resistance to extension (B.U.). 45min 90min 135min. 560 610 700. 620 730 780. 670 900 1000. 740 1000 1000. 880 1000 1000. 860 1000 1000. Area under curve (cm2). 45min 90min 135min. 133 124 149. 140 146 156. 150 162 185. 170 -1) -. 173 -. 182 -. Water absorption (%). -1): Unmeasured.. Fig. 8. Effects of silkpeptide concentration on R/E (resistance/ extension) ratio of dough.. Fig. 7. Extensograms of dough added with various levels of silkpeptide (SP).. j Ï Î&º >#~ bWö ~º 'Ëj GöB " r ÖzB Î& j ¾æÚÚ VËW Î" ¢ &ê Â BBïBê 3;' Î"& ®j © .. º. £. Ï~ Wîf 90.83% ï Ö ¸~ C jÖ ïf 50,224.12 mg% Ö ¸~ . jÖ Wf glycine(37.4%) B¢ ô~b alanine(28.2%), serine (14.7%) 5 tyrosine(8.6%) Bb ¾æÒ C ïf *. Ú jÖ ï~ 89% ¸f jNj Næ~& . Ï ~ ª¶ïf 1500-1600 Dab G;>îb, «¶Vº 1045 µm «¶V& ·~& . >#~ bÒ' ßW farinographöB >#ê*f Ï Î&ï Ã& & ö j * ² Ë>îb >#;W*f ^Úr . n;êº Ï 2.0% Î&ræº &f jÝ n; ê¢ &b¾ 3.0%, 4.0% Ã& n;êº Ô~ £zê º £* Ã&~& . Amylogram ßWöB ^zB Nêº 100% && &º 59.5oCîb Ï 3.0% Î &ræº &f ÿ¢~&, 4.0% Î&º 58.0oC & Ô~ . 6êNêöB Ï Î&f & º N¢ æ p~b 6êº Ï Ã& 6 ²~º ãËj & . ExtensographöB Ï Ã& > #~ &êº ² Ã&~& Ëê~ 8ê *~ ã"ö V¢ Ã&~& . ß® 2.0% ç Î&~ 90ª ê¦Vº & ê 8 ² Ã&~ G;8j ¾æâ >& ìî . Ë êf &ê 8~ jN R/E8~ æzº Ï Ã&ö V¢ * ã" R/E8f Ã&~&b, Ï¢ Î& ~º ãÖº >#~ &Ê FK" BÎ ÚK &&ò Ò Ï ãÖ º ² Ã&>Ú ÖzB¢ Î& ># bWj Ï Î&º >#~ bWö ~º 'Ëj G.

(9) ®"²æ B 36 ² B 2 ^ (2004). 254. öB " r ÖzB j ¾æÚÚ VËWj &ê Â B BïBê 3;' Î"& ®j © .. 6Ò~ ¢^f 2003jê B*& FWj~ æöö ~ >îb ö 6Òãî .. ^. ò. 1. Chen K, Umeda Y, Hirabayash K. Enzymatic hydrolysis of silk fibroin. Jpn. J. Sericult. Sci. 65: 131-133 (1995) 2. Guoding C, Mitsuo A, Kiyoshi H. Isolation of tyrosine from silk fibroin by enzyme hydrolysis. Jpn. J. Sericult. Sci. 65: 182-184 (1996) 3. Sugiyama K, Kushima Y, Muramatsu K. Effect of sulfur containing amino acids and glycine on plasma cholesterol level in rats fed on a high cholesterol diet. Agric. Biol. Chem. 49: 3455-3461 (1985) 4. Takano R, Chen K, Hirabayashi K. Production of soluble fibroin powder by hydrolysis with hydrochloric acid and physical properties. Jpn. J. Sericult. Sci. 60: 358-362 (1991) 5. Yoshikawa M, Chiba H. Frontiers and new horizons in amino acid research. Jpn. J. Sericult. Sci. 61: 403-406 (1992) 6. Luo J, Chen K, Xu Q, Hirabayashi K. Study on foodization of fibroin and its functionality: The 2nd international silk conference. 1: 73-87 (1993) 7. Keiko F, Sadayuki T, Rumiko K. Preparation and properties of a novel sponge cake by combining rice flour with silk fibroin protein. Jpn. J. Soc. Food Sci. Technol. 47: 363-367 (2000) 8. AOAC. Official Methods of Analysis. 15th ed. Association of Official Analytical Chemists, Washington, DC, USA (1990) 9. Prosky L, Asp NG, Furda I, Devreis JW, Scjweozer TF, Harland BA. Determination of total dietary fiber in foods and food products. J. Assoc. Off. Anal. Chem. 68: 677-684 (1987) 10. Bidlingmeyer BA, Cohen SA, Taruin TL, Frost B. A new rapid. high sensitivity analysis of amino acid in food type samples. J. Assoc. Off. Anal. Chem. 70: 241-253 (1987) 11. AACC. Approved Method of the AACC. Method 54-21. American Association of Cereal Chemists, St. Paul, MN, USA (1985) 12. AACC. Approved Method of the AACC. Method 22-10. American Association of Cereal Chemists, St. Paul, MN, USA (1985) 13. AACC. Approved Method of the AACC. Method 54-10. American Association of Cereal Chemists, St. Paul, MN, USA (1985) 14. Magoffin CD, Hoseney RC. A review of fermentation. Baker's Digest. 48: 22-29 (1974) 15. Kim CT, Cho SJ, Hwang JK, Kim CJ. Composition of amino acid, sugars and minerals of domestic wheat varieties. Korean J. Soc. Food Sci. Nutr. 26: 229-235 (1997) 16. Nahm JH, Oh YS. Study of pharmacological effect of silk fibroin. J. Agri. Sci. 37: 145-157 (1995) 17. Kwon HR, Ahn MS. Study on rheological and general baking properties of breads and their rusks prepared of various flour. Korean J. Food Sci. Technol. 11: 479-486 (1995) 18. Parades-Lopez O, Bushuk W. Development and undevelopment of wheat dough by mixing microscopic structure and its relations to bread-making quality. Cereal Chem. 60: 24-27 (1982) 19. Parkkonen T, Harkonen H, Autio K. Effect of baking on the microstructure of rye cell walls and protein. Cereal Chem. 71: 58-63 (1994) 20. Pomeranz Y, Mayer D, Seible W. Wheat, rye and dough scanning electron microscopy. Cereal Chem. 61: 53-69 (1984) 21. Kim DH. Food Chemistry. Tamgudang, Seoul, Korea. pp. 289294 (1988) 22. Hoseney RC, Hsu KH, Junge RC. A simple spread test to measure the rheological properties of fermenting dough. Cereal Chem. 56: 141-152 (1979) 23. Cho NJ, Hur DK, Kim SK. The effect of ascorbic acid and Lcystein on rheological properties of wheat flour and no-time dough method. Korean J. Food Sci. Technol. 21: 800-807 (1989) 24. Elkassabany M, Hoseney RC. Ascorbic acid as an oxidant in wheat flour dough II. Rheological effects. Cereal Chem. 57: 8895 (1980) (2003j 11ú 13¢ 7>; 2003j 12ú 24¢ j).

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