본문 바로가기 주메뉴 바로가기
국회도서관 홈으로 정보검색 소장정보 검색

결과 내 검색

동의어 포함

목차보기

목차

표제지=0,1,1

최종보고서/김병기=i,2,2

제출문=iii,4,1

연구보고서 목차=iv,5,3

표 목차=vii,8,3

그림목차=x,11,5

요약문=xv,16,9

SUMMARY=xxiv,25,8

1. 서론=1,33,3

2. 연구목표, 연구내용 및 범위=4,36,3

3. 연구범위 및 연구수행 방법=7,39,1

3.1. 새로운 대두유지 추출방법의 개발 및 대두박의 품질평가=7,39,1

3.1.1. 대두=7,39,1

3.1.2. 초미세여과(ultrafiltration) 예비실험=7,39,2

3.1.3. 분석=8,40,4

3.2. 막분리처리에 의한 대두단백질 분리기술 확립=12,44,1

3.2.1. 재료=12,44,1

3.2.2. 대두 단백질 추출조건의 최적화=12,44,1

3.2.3. 농축대두단백 생산=12,44,3

3.2.4. 분석방법=14,46,4

3.3. 단백질 분해효소의 선별 및 단백질 가공용 효소의 개발=17,49,1

3.3.1. 사용배지 및 시약=17,49,2

3.3.2. 균주분리 및 선발=18,50,2

3.3.3. 미생물의 동정=19,51,2

3.3.4. 효소활성의 측정=20,52,2

3.3.5. 균체의 생산 및 효소 생산조건의 검토=21,53,1

3.3.6. 효소정제=21,53,2

3.4. 고단백 가공식품의 제조=22,54,1

3.4.1. 단백질 분해효소를 이용한 식물성치즈의 제조=22,54,6

3.4.2. 고단백 스넥제품 개발=27,59,1

3.5. 대두단백질 발효조건 확립=28,60,1

3.5.1. 향미증강용 소재탐색=28,60,1

3.5.2. 향미증강 된장제조=28,60,3

3.5.3. 향미증강 고추장 제조=31,63,1

3.5.4. 향미증강 양조간장 제조 및 응용제품 개발=31,63,3

3.6. 대두단백질 발효조건 확립을 위한 대두발효식품의 향기성분 분석=33,65,1

3.6.1. 대두발효식품의 휘발성 향기성분 추출=33,65,2

3.6.2. Gas chromatography-mass spectrometry(GC-MS)=34,66,2

3.6.3. Gas chromatography-olfactometry(GC-O)=35,67,1

3.6.4. Aroma Extraction Dilution Analysis(AEDA)=35,67,1

3.6.5. 향기성분의 동정=35,67,2

3.7. 향미증강 양조간장의 향기성분 분석=36,68,1

3.7.1. 재료=36,68,1

3.7.2. 용매추출법(direct solvent extraction)=36,68,1

3.7.3. Gas chromatography-mass spectrometry-olfactometry=37,69,1

3.7.4. 휘발성 향기성분의 동정=37,69,1

3.7.5. Model solution의 solid phase microextraction(SPME)=37,69,2

3.7.6. 향미증강 양조간장의 SPME-GC-O=38,70,4

4. 연구수행 내용 및 결과=42,74,1

4.1. 새로운 대두성분 추출방법의 개발 및 대두박의 품질 평가=42,74,1

4.1.1. 추출공정 디자인 및 최적화=42,74,1

4.1.2. 원료 및 제품분석=42,74,2

4.1.3. AEP 추출성분의 분리=43,75,3

4.2. 막분리기술에 의한 대두단백질 분리기술 확립=46,78,1

4.2.1. 농축대두단백의 일반성분=46,78,3

4.2.2. 단백질추출조건의 최적화=49,81,3

4.2.3. 농축대두단백 생산=52,84,2

4.2.4. 농축대두단백의 기능성(functional properties)=53,85,8

4.2.5. 농축대두단백의 이화학적 특성=60,92,13

4.3. 단백질 분해효소의 선별 및 단백질가공용 효소의 개발=73,105,1

4.3.1. Bacillus sp. 218이 생산하는 내열성 단백질분해효소=73,105,13

4.3.2. Bacillus sp. JE 375가 생산하는 단백질분해효소=85,117,39

4.3.3. Bacillus sp. DK1122가 생산하는 호알카리성 단백질 분해효소=123,155,8

4.3.4. 결론=130,162,6

4.4. 고단백 가공식품의 제조=136,168,1

4.4.1. 단백질분해효소를 이용한 식물성치즈의 개발=136,168,6

4.4.2. 고단백 스넥제품 개발=141,173,16

4.5. 대두단백질 발효조건 확립=157,189,1

4.5.1. 항미향상 소재탐색=157,189,1

4.5.2. 향미증강 된장제조=157,189,16

4.5.3. 향미증강 소스베이스용 간장개발=172,204,4

4.5.4. 연구성과=175,207,8

4.6. 대두단백질 발효조건 확립을 위한 대두발효식품 향기성분분석=183,215,1

4.6.1. 간장=183,215,2

4.6.2. 고추장=184,216,14

4.6.3. 된장=197,229,2

4.6.4. 청국장=198,230,2

4.6.5. 향미증강 양조간장 향기성분 분석=199,231,12

참고문헌=211,243,11

표목차

Table 1. Operation conditions for the texture profile analysis of soybean cheese=25,57,1

Table 2. Formulation for wheat snack sample preparations=26,58,1

Table 3. Ingredients formulations for kochujang=30,62,1

Table 4. Proximate composition of dehulled soybean halves=40,72,1

Table 5. Distribution of soybean solids and nitrogen in membrane separation conditions at various particle size and water-to-bean ratio at pH 7.0=41,73,1

Table 6. Proximate composition of soy protein concentrates obtained by different manufacturing procedures=45,77,1

Table 7. Distribution of soybean solids and nitrogen in membrane extraction conditions as affected by sonication time=48,80,1

Table 8. Amino acid composition of three protein samples and commercial soy protein concentrate=61,93,1

Table 9. Color evaluation of soy protein concentrates=63,95,1

Table 10. Residual trypsin inhibitor activity in the representative protein products and raw soybeans=64,96,1

Table 11. Physiological and biochemical characteristics of the strain DF 218=69,101,1

Table 12. Cell wall fatty acid composition of the strain DF218=70,102,1

Table 13. Purification of the protease from Bacillus sp. DF 218=79,111,1

Table 14. Basic biochemical and physiological characteristics of the Strain JE 375=87,119,1

Table 15. Cell wall fatty acid composition of the strain JE 375=88,120,1

Table 16. Medium composition for the production of the pretense from Bacillus sp. JE 375=101,133,1

Table 17. Effect of type and concentration of solvent on the precipitation of the enzyme produced by Bacillus sp. JE 375=103,135,1

Table 18. Purification of protease from Bacillus sp. JE 375=106,138,1

Table 19. Other characterlstics of Bacillus sp. DK1122=121,153,1

Table 20. Effect of starter on curd formation of protease treated soymilk=133,165,1

Table 21. Effect of enzyme concentration on color and textural properties of soy cheese=134,166,1

Table 22. Effect of protease and starter on color, textural property and pH of soy cheese=135,167,1

Table 23. Proximate analysis of raw mix for wheat snack production=139,171,1

Table 24. Optimum operating conditions for X-25 Wenger extruder=140,172,1

Table 25. Flavor enhancing materials(condiments and herbs) and their medicinal effects=153,185,1

Table 25. Comparison of amylase activity in soybean koji with different ingredients=154,186,1

Table 27. Comparison of protease activity in soybean koji with different ingredients=155,187,1

Table 28. Comparison of β-glucosidase activity in soybean koji with different ingredients=156,188,1

Tabte 29. Comparison of iso-flavone activity in soybean koji with different ingredients=158,190,1

Table 30. Isoflavone contents in soybean paste made of koji with added flavor-enhancing raw materials=160,192,1

Table 31. Sensory evaluation results of soybean paste made of koji with added flavor-enhancing raw materials=161,193,1

Table 32. Sensory evaluation results of hot paste(kochujang) made of koji with added flavor-enhancing herbs=163,195,1

Table 33. Comparison of amylase activities in meju and the resulting soybean sauce during processing periods=164,196,1

Table 34. Comparison of protease activlties in meju and the corresponding soybean sauce during processing periods=166,198,1

Table 35. Comparison of β-glucosidase activities in meju and the resulting soybean sauce during processing periods=167,199,1

Table 36. Comparison of isoflavone in meju and the resulting soybean sauce during processing periods=168,200,1

Table 37. Comparison of free amino acids in soybean embryo-enriched soy sauce and a commercial fermented product sold in the market=169,201,1

Table 38. Sensory evaluation scores for the flavor-enhanced fermented soy sauce=170,202,1

Table 39. Volatile flavor compounds identified from soy sauce=177,209,1

Table 40. Aroma-active compounds detected from soy sauce=178,210,1

Table 41. Volatile flavor compounds identified from kochujang=181,213,2

Table 42. Aroma-active compunds detected from kochujang=186,218,1

Table 43. Volatile flavor compounds identified from doenjang=188,220,1

Table 44. Aroma-active compounds detected from doenjang=189,221,1

Table 45. Volatile flavor compound identified from chungkookjang=191,223,1

Table 46. Aroma-active compounds of chungkookjang=192,224,1

Table 47 Volatile flavor compounds identified from flavor-enriched soy sauces=193,225,2

Table 48. Aroma-active compounds from flavor-enriched soy sauces=195,227,1

Table 49. Aroma-active compounds from flavor-enhanced soy sauces by SPME-GC-O=209,241,1

Figure 1. Flow diagram showing extraction processing of soybean to produce soy protein concentrate by ultrafiltration membrane treatment=9,41,1

Figure 2. System schematic for the membrane concentration of soy proteins=10,42,1

Figure 3. Flow diagram showing extraction processing of soybean to produce soy protein concentrate by acid precipitation procedures=11,43,1

Figure 4. A flow diagram showing extraction processing of soybean to produce protein isolate and oil using ultrafiltration membranes=39,71,1

Figure 5. Extractable soybean solids at various particle sizes and solid-to-water ratios at pH 7=47,79,1

Figure 6. Nitrogen solubilities of protein samples obtained by membrane filtration at pH 7.0 and acid precipitation procedures=50,82,1

Figure 7. Heat coagulation properties of protein samples obtained by membrane filtration at pH 7.0 and acid precipitation procedures=51,83,1

Figure 8. Emulsion capacities of protein samples obtained by membrane filtration at pH 7.0 and acid precipitation procedures=55,87,1

Figure 9. Emulsion stabilities of protein samples obtained at pH 7.0 by membrane filtration and acid precipitation procedures=56,88,1

Figure 10. Foaming capacities of protein samples obtained by membrane filtration at pH 7.0 and acid precipitation procedures=58,90,1

Figure 11. Foaming stabilities of protein samples obtained by membrane filtration at pH 7.0 and acid precipitation procedures=59,91,1

Figure 12. Sodium Dodecyl Sulfate polyacrylamide gel electrophoretic patterns of protein samples=62,94,1

Figure 13. Formation of digestion clear zone in the LB media containing 2% casein powder=67,99,1

Figure 14. Scanning electron micrograph of the strain DF 218=68,100,1

Figure 15.165 rDNA sequence of strain DF 218(1,602bases)=71,103,1

Figure 16. Dendrogram of the Bacillus sp. DF 218 through 165 rDNA gene sertuence aomology=72,104,1

Figure 17. Effect of culture temp on the growth of Bacillus sp. DF 218=74,106,1

Figure 18. Effect of culture time on the growth and protease production from Bacillus sp. DF 218=75,107,1

Figure 19. Effect of initial pH of medium on the growth and production of the protease from Bacillus sp. DF 218=76,108,1

Figure 20. DEAE-sepharose column chromatogram of protease from Bacillus sp. DF 218=77,109,1

Figure 21. SDS-PAGE of the protease from Bacillus sp. DF 218=78,110,1

Figure 22. Effect of initial pH on the protease production from Bacillus SP. Df 218=82,114,1

Figure 23. Effect of temp on the protease production from Bacillus sp. DF 218=83,115,1

Figure 24. Scanning electron micrograph of the strain JE 375=84,116,1

Figure 25. Formation of digestion clear zone on the LB media containing 2% skim milk=86,118,1

Figure 26. Whole cell fatty acid composition of strain JE 375 by gas chromatography=89,121,1

Figure 27. 165 rDNA sequence of strain JE 375(1,846 base)=90,122,1

Figure 28. Dendrogram of the Bacillus sp. JE 375 through 16S rDNA gene sequence homology=91,123,1

Figure 29. Comparison of 16S rDNA sequence among strain JE 375. B. caldoxylolyticus and B. thermoglucosidasius=92,124,1

Figure 30. Effect of culture temp on the growth and enzyme production of Bacillus sp. JE 375=96,128,1

Figure 31. Effect of culture time on the growth and enzyme production of doenjang sp.JE 375=97,129,1

Figure 32. Effect of initial pH of medium on the growth and enzyme production of Bacillus sp. JE 375=98,130,1

Figure 33. The growth and enzyme production of Bacillus sp. JE 375 depending on carbon sources(%)=99,131,1

Figure 34. The growth and enzyme production from nitrogen sources(1%. w/v) by Bacillus sp. JE 375=100,132,1

Figure 35. Profiles of cell growth, pH, protein concentration and production of the enzyme of Bacillus sp. JE 375=102,134,1

Figure 35. Chromatogram of the protease on DSAE-sepharose column=104,136,1

Figure 37. SDS-PAGE of protease from Bacillus sp. JE 375=105,137,1

Figure 38. Effect of initial pH on the enzyme production from Bacillus sp. JE 375=112,144,1

Figure 39. Effect of temperatue on the enzyme production from Bacillus sp. JE 375=113,145,1

Figure 40. Effect of inorganic salts on the enzyme production from Bacillus sp. JE 375=114,146,1

Figure 41. Effect of concentration of Cac12 on the enzyme activity of Bacillus sp. JE 375=115,147,1

Figure 42. Effect of amino acid modifying reagents and detergents on enzyme activity from Bacillus sp. JE 375=117,149,1

Figure 43. Effect of concentration of cystein and iodoacetamide on the enzyme activity from Bacillus sp. JE 375=118,150,1

Figure 44. pH stability for enzyme activity from fociffur sp. JE 375=120,152,1

Figure 45. Dendrogram of the Bacillus sp. Dkl122 through 165 rBNA gene sequence homology=122,154,1

Figure 46. Effect of culture temp on the growth and enzyme activity of Bacillus sp. DK1122=124,156,1

Figure 47. Effect of culture pH of medium on the growth and enzyme activity of Bacillus sp. BK1122=125,157,1

Figure 48. Effect of culture NaCl cone.(C) on the growth and enzyme activity of Bacillus sp. DK1122=126,158,1

Figure 49. Chromatogram of Iytic enzyme from DK1122 on CM-agarose column=127,159,1

Figure 50. SDS-PAGE of Iytic enzyme from DK1122=128,160,1

Figure 51. Changes in bulk density of wheat-snack products as affected by the added tuna meat=143,175,1

Figure 52. Changes in brittleness of wheat-snack products as affected by the added tuna meat=144,176,1

Figure 53. Changes in hardness of wheat-snack products as affected by the added tuna meat=145,177,1

Figure 54. Changes in Hunter colorimetric "L" values of wheat-snack products as affected by the added tuna meat=147,179,1

Figure 55. Changes in Hunter colorimetric "a" values of wheat-snack products as affected by the added tuna meat=148,180,1

Figure 56. Changes in Hunter colorimetric "b" values of wheat-snack products as affected by the added tuna meat=149,181,1

Figure 57. Slectron micrographs of extruded wheat-snack products with(upper) and without(lower) added tuna meat=150,182,1

Figure 58. Total ion chromatogram of volatile flavor compounds isolated from soy sauce=176,208,1

Figure 59. Flavor dilution chromatogram of soy sauce extracted by vacuum SDE=179,211,1

Figure 60. Total ion chromatogram of volatile flavor compounds of kochujang=180,212,1

Figure 61. Total ion chromatogram of volatile flavor compounds of deonjang=187,219,1

Figure 62. Total ion chromatogram of volatile flavor compounds of chungkookjang=190,222,1

Figure 63. Comparison of peak area ratio of 2-ethyl-4-hydroxy-5-methyl-3(2H)-furanone(HEMF) from flavor-enhanced soy sauces=196,228,1

Figure 64. GC response for each standard with different concentration (ppm) by PDMS fiber=203,235,1

Figure 65. Flavor dilution chromatogram of volatiles isolated from commercial soy sauce by SPME-GC-O=204,236,1

Figure 66. Flavor dilution chromatogram of volatiles isolated from cinnamon flavor-enriched soy sauce by SPME-GC-O=205,237,1

Figure 67. Flavor dilution chromatogram of volatiles isolated from rosemary flavor-enriched soy sauce by SPME-GC-O=206,238,1

Figure 68. Flavor dilution chromatogram of volatiles isolated from thyme flavor-enriched soy sauce by SPME-GC-O=207,239,1

Figure 69. Flavor dilution chromatogram of volatiles isolated from clove flavor-enriched soy sauce by SPME-GC-O=208,240,1