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論文名稱: | Aeromonas salmonicida MAEF108 所產 Agarase AS-II 之純化與特性研究暨經 Agarase AS-II 水解所得藻類寡醣之生理活性探討
| Studies on Purification and Characterization of Aeromonas salmonicida MAEF108 Agarase AS-II and Bioactivities of Agarase AS-II Digested Algal Oligosaccharides
研究生: | 康新楷 Sheen-Kye Kang
指導教授: | 潘崇良 博士 Chorng-Liang Pan, Ph.D.
學位類別: | 碩士
學校名稱: | 國立臺灣海洋大學
系所名稱: | 食品科學系
學號: | M94320030
畢業學年度: | 95
語文別: | 英文
關鍵字: | 洋菜□ agarase
| 藻類 algae
| 生理活性 bioactivity
全文點閱次數: | 31

全文影像連結:

論文全文(pdf)

論文頁數: | 156
摘要: | 從海洋細菌 Aeromonas salmonicida MAEF108 所產具有洋菜□活性劃分中純化單一酵素，命名為Agarase AS-II 並且利用此一純化酵素降解龍鬚菜或海菜萃取多醣評估其生理活性。A. salmonicida MAEF108 培養液經離心 (30,700 x g)、超過濾 (30 kDa MWCO)、以及離子交換層析得到 Agarase AS-II，其純化倍率為 44.03，經電泳分析後得到分子量估計為 95.4 kDa 的單一蛋白質。Agarase AS-II 的最適作用溫度以及 pH 分別為 45oC 及 7.0, 且存放在低於 40oC 2 小時之後仍具有 60% 以上的殘存活性；存放於 pH 6.0-8.0 的磷酸緩衝溶液中有較佳的穩定性。與不添加金屬離子的控制組相比，5 mM CaCl2 可以增加 Agarase AS-II 30% 的酵素活性。Agarase AS-II 的活化能與 Km 分別為 46.24 J mol-1 K-1 及 4.39% 的 agarose 基質。此純化酵素對紅藻綱藻類及其精製萃取物具有基質特異性，並可在 1 分鐘時即已水解部分 agarose，且生成以新洋菜六醣 (neoagarohexaose, N6) 以及新洋菜四醣 (neoagarotetraose, N4) 組成的最終產物，因此被認為是一個可將 agarose 直接水解產生 N6 及 N4 的 beta-agarase。除此之外，Agarase AS-II 具有將 N2 生合成 N4 以及將半乳糖生合成未知寡聚合物的能力。
| 以 2 mg/mL 的 (1) 龍鬚菜萃取多醣 (Gra) 或海菜萃取多醣 (Mon)、(2) Gra 或 Mon 經 A. salmonicida MAEF108 粗酵素液降解所得降解物 (Gra-C108、Mon-C108)、以及 (3) Gra 或 Mon 經 Agarase AS-II 降解所得降解物 (Gra-AS-II、Mon-AS-II) 等做為三株雙歧桿菌 (bifidobacteria) 的生長碳源，以評估做為益生物質的能力。當 Bifidobacterium pseudolongum subsp. pseudolongum BCRC 14673 利用 Gra-C108 時，24 小時之內活菌數可以增加到超過 3 log cfu/mL。海菜萃取多醣及其水解物亦皆能夠做為雙歧桿菌生長利用的碳源。B. adolescentis BCRC 14608 以及 B. pseudolongum subsp. pseudolongum BCRC 14673 皆可利用上述 6 種藻類樣品且產酸降低 pH 值。B. longum BCRC 11847 較能利用龍鬚菜樣品產酸降低 pH 值。不同濃度的 6 種海藻樣品 (Gra、Mon、Gra-C108、Mon-C108、G-AS-II、或 Mon-AS-II) 分別與不同濃度的BHK-21 細胞進行培養，發現皆不具細胞毒性，且細胞存活率皆高於 78%。6 種藻類樣品均呈現降低日本腦炎病毒北京一型感染 BHK-21 細胞的現象，且硫酸根含量較高之海菜樣品降低感染的能力優於龍鬚菜樣品。龍鬚菜或海菜萃取多醣經 A. salmonicida MAEF108 粗酵素液或 Agarase AS-II 降解後，均可測得較多的多酚類化合物及硫酸根含量之產物。龍鬚菜樣品 Gra-C108 與 Gra-AS-II 分別具有 93.10% 和 78.49% 的螯合能力，高於 Gra (62.52%) 以及 Mon (21.25%)。
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| Agarase AS-II was purified from the four fractions having agarase activities of marine bacteria Aeromonas salmonicida MAEF108 agarases, and was used to digest Gracilaria sp. or Monostroma nitidum extracted polysaccharides to evaluate its bioactive properties.  Culture suspension of A. salmonicida MAEF108 was centrifuged (30,700 x g), ultrafiltration (30 kDa MWCO), then applied to ion-exchange chromatography to obtain Agarase AS-II which was 44.03-fold purified and was estimated as a 95.4 kDa single protein.  The optimal temperature and pH to degrade 0.2% agarose were 45oC and 7.0, respectively.  It maintained 60% residual activity when Agarase AS-II was stored below 40oC for 2 hours; the stability of Agarase AS-II was better when stored in pH 6.0-8.0 phosphate buffer.  The addition of 5 mM CaCl2 in assay buffer could contribute 30% higher relative activity than no metal ions were added.  Activation energy and Km of Agarase AS-II were 46.24 J mol-1 K-1 and 4.39% of agarose, respectively.  The purified agarase has substrate specificity on Rhodophyta and its refined products, and could degrade agarose into final products of neoagarohexaose (N6) and neoagarotetraose (N4), indicating that Agarase AS-II could be regarded as a beta-agarase which would directly degrade agarose to produce N6 and N4.  In addition, Agarase AS-II has the abilities to biosynthesize N4 and unidentified galactose oligomers from neoagarobiose (N2) and galactose, respectively.
| 2 mg/mL of (1) either Gracilaria sp. extracted polysaccharides (Gra) or M. nitidum extracted polysaccharides (Mon),  Gra or Mon digested by A. salmonicida MAEF108 crude agarases (Gra-C108 and Mon-C108), or (3) Gra or Mon digested by Agarase AS-II (Gra-AS-II or Mon-AS-II) was tested as a carbon source for bifidobacteria growth to evaluate prebiotic potentials.  Viable bacteria counts of Bifidobacterium pseudolongum subsp. pseudolongum BCRC 14673 could increase more than 3 log cfu/mL in 24 hour-incubation when Gra-C108 was utilized.  M. nitidum extracted polysaccharides and its agarase lysates were also able to be utilized by bifidobacteria as carbon source.  B. adolescentis BCRC 14608 and B. pseudolongum subsp. pseudolongum BCRC 14673 could utilize 6 algal samples to lower pH.  B. longum BCRC 11847 performed better pH lowering ability when utilizing Gracilaria sp. based samples.  Different concentrations of 6 algal samples (Gra, Mon, Gra-C108, Mon-C108, Gra-AS-II, or Mon-AS-II) were cultured with different cell densities of BHK-21 kidney cells in which the algal samples showed no cytotoxicity and the cell viability was higher than 78%.  The 6 algal samples showed ability to decrease the effects caused by Japanese Encephalitis Virus (JEV, Beijing-1 strain) infection.  It was found that M. nitidum based samples performing better antiviral activity than Gracilaria sp. based samples was due to having higher sulfated group contents.  Gra or Mon digested by either A. salmonicida MAEF108 crude agarases or Agarase AS-II, could obtain products containing higher amount of polyphenolic compounds and sulfated group.  Gra-C108 and Gra-AS-II performed 93.10 and 78.49% chelating effects on Fe2+, respectively, which were higher than those of Gra (62.52%) or Mon (21.25%).
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論文目次: | Table of Contents
|
| Contents    i
| List of Tables    v
| List of Figures    vi
| List of Appendix    x
| Chinese abstract    xi
| Abstract    xiii
|
| Introduction    1
| Literature Review    3
| 1.  Agarase    3
| 1.1  Source of agarase producing bacteria    4
| 1.2  Biochemical properties of agarase    4
| 1.2-(1)  Optimal pH and optimal temperatures    4
| 1.2-(2)  Molecular mass    4
| 1.2-(3)  Cations    5
| 2.  Algal polysaccharides    6
| 2.1  Agar    6
| 2.2  Gracilaria sp. polysaccharides    7
| 2.2-(1)  General information of the seaweed    7
| 2.2-(2)  Bioactivities    7
| 2.2-(2)-A  Antivirus activity    7
| 2.2-(2)-B  Antibacterial activity    8
| 2.3  Monostroma nitidum polysaccharides    8
| 2.3-(1)  Sources and components    8
| 2.3-(2)  Bioactivities    9
| 2.3-(2)-A  Blood cholesterol-lowering agent    9
| 2.3-(2)-B  Anticoagulant    9
| 2.3-(2)-C  Antivirus activity    10
| 3.  Algal polysaccharide lysates    10
| 4.  Algal polysaccharide lysate identification    11
| 4.1  Thin-layer chromatography (TLC)    11
| 4.2  High performance liquid chromatography (HPLC)    12
| 4.3  Nuclear magnetic resonance (NMR)    13
| 5.  Affection of oligosaccharides to gut health    14
| 5.1  Prebiotics    14
| 5.2  Characterisics of oligosaccharides    14
| 5.3  Bifidobacteria and their beneficial effects on human health    15
| 6.  Antioxidant properties of algal polyphenols    16
| 7.  Antiviral properties from algae and carbohydrates    18
| 8.  Japanese Encephalitis Virus (JEV)    19
|
| Experimental Design    21
| Materials and Methods    22
| I.  Materials    22
| I-1  Seaweed materials    22
| I-2  Agarase producing bacteria strain    22
| I-2-(1)  Strain preservation    22
| I-2-(2)  Inoculumn preparation    23
| I-3  Cell line and virus strain    23
| I-3-(1)  Hamster kidney cells    23
| I-3-(2)  Culture and preservation    23
| I-3-(2)-A  Cell line culture    23
| I-3-(2)-B  Cell line preservation    24
| I-3-(3)  Japanese Encephalitis Virus (JEV)    24
| I-4  Bacteria for evaluating prebiotic abilities    24
| I-5  Chemical reagents    24
| I-6  Medium    27
| I-7  Experimental equipments    28
| II.  Methods    30
| II-1  A. salmonicida MAEF108 crude agarases preparation    30
| II-1-(1)  Crude agarases preparation    30
| II-1-(2)  Measurements and definition of agarase activities    31
| II-2  A. salmonicida MAEF108 agarases purification    31
| II-2-(1)  Purify procedure    31
| II-2-(1)-A  Concentration via ultrafiltration    31
| II-2-(1)-B  Ion-exchange    31
| II-2-(2)  Identification of physical properties    32
| II-2-(2)-A  SDS-polyacrylamide gel electrophoresis    32
| II-2-(2)-B  N-terminal amino acid sequence    33
| II-2-(2)-C  Internal sequencing    33
| II-2-(3)  Biochemical properties    33
| II-2-(3)-A  Optimal temperature    33
| II-2-(3)-B  Optimal pH    33
| II-2-(3)-C  Thermal stability    34
| II-2-(3)-D  pH stability    34
| II-2-(3)-E  Metal ions    34
| II-2-(3)-F  Artificial sea water (ASW)    34
| II-2-(3)-G  Storage stability    35
| II-2-(3)-H  Activation energy    35
| II-2-(3)-I  Determination of the enzyme kinetic curve    35
| II-2-(3) J  Substrate specificity    35
| II-2-(3)-K  Cleavage properties and mode of action    36
| II-2-(3)-L  Simple sugar biosynthesis    36
| II-3  Algal polysaccharide extraction    36
| II-3-(1)  Gracilaria sp. and Monostroma nitidum
| polysaccharide extraction    36
| II-3-(2)  Total sugar content    37
| II-4  Algal polysaccharide lysate preparation    37
| II-4-(1)  Gracilaria sp. or Monostroma nitidum
| polysaccharide agarase lysates preparation    37
| II-4-(2)  Sulfated group contents quantification    38
| II-4-(2)-A  Reagents    37
| II-4-(2)-B  Sample treatment    37
| II-4-(2)-C  Sulfated group content quantification    38
| II-4-(3)  Algal polysaccharide agarase lysate analysis    38
| II-4-(3)-A  Gel permeation chromatography (GPC)    38
| II-4-(3)-B  Thin layer chromatography (TLC)    38
| II-4-(3)-C  High performance liquid chromatography (HPLC)    39
| II-4-(3)-D  Nuclear magnetic resonance (NMR)    39
| II-4-(4)  Cell viability and antivirus    39
| II-4-(4)-A  MTT assay    39
| II-4-(4)-B  Antivirus    40
| II-4-(5)  Prebiotic potential evaluation    40
| II-4-(6)  Antioxidative properties    40
| II-4-(6)-A  Polyphenol quantification    40
| II-4-(6)-B  Ferrous-chelating antioxidant power    41
|
|
| Results and Discussions    42
| 1. Aeromonas salmonicida MAEF108 Agarase AS-II purification    42
| 2. Aeromonas salmonicida MAEF108 Agarase AS-II identification    43
| 3. Characteristics of A. salmonicida MAEF108 Agarase AS-II    45
| 3-(1)  Optimal temperature    45
| 3-(2)  Optimal pH    45
| 3-(3)  Thermal stability    46
| 3-(4)  pH stability    47
| 3-(5)  Metal ions    47
| 3-(6)  Artificial seawater    48
| 3-(7)  Storage stability    49
| 3-(8)  Activation energy and kinetic properties    49
| 3-(9)  Substrate specificity    50
| 3-(10)  Cleavage properties and biosynthesis    50
| 4. Bioactive properties of two algal extracted polysaccharides
| and their lysates    53
| 4-(1) Composition    53
| 4-(2) Prebiotic evaluation    55
| 4-(3) Cell viability and anti-JEV abilities    56
| 4-(4) Antioxidative properties    58
|
| Conclusions    60
| Bibliography    63
| Tables    78
| Figures    83
| Appendix    131
|
| List of Tables
|
| Table 1        Purification of Agarase AS-II from A. salmonicida MAEF108    78
| Table 2    Effects of metal ions on Agarase AS-II activity    79
| Table 3    Storage stability of Agarase AS-II during a 14-day test    80
| Table 4    Sulfated group contents and 50% inhibitory concentration (IC50) of two algal extracted polysaccharides or their agarase lysates of JEV infection    81
| Table 5    Polyphenolic compound contents and Fe2+ ion chelating effects of two algal extracted polysaccharides or their agarase lysates    82
|
| List of Figures
|
| Figure 1        Ion-exchange chromatography of Aeromonas salmonicida MAEF108 crude agarases    83
| Figure 2        12% SDS-PAGE pattern of crude agarase samples produced by Aeromonas salmonicida MAEF108 during each purification steps    84
| Figure 3        Effects of temperature on the activity of Agarase AS-II    85
| Figure 4        Effects of pH on the activity of Agarase AS-II    86
| Figure 5        The effects of temperature on the stability of Agarase AS-II    87
| Figure 6        The effects of pH on the stability of Agarase AS-II    88
| Figure 7        Relative activity of Agarase AS-II under different concentrations of artificial seawater (ASW)    89
| Figure 8        Arrhenius plot established from digesting 0.2% agarose degraded by 100 □L Agarase AS-II (0.036 U) at 35oC, 40oC, 45oC, and 50oC for 10 minutes    90
| Figure 9        The kinetic properties of Agarase AS-II    91
| Figure 10        Substrate specificity of Agarase AS-II among fourteen algal substrates    92
| Figure 11        TLC profile of agarose degraded by Agarase AS-II for 0-48 hours    93
| Figure 12        TLC profile of agarose degraded by Agarase AS-II for 0-10 minutes    94
| Figure 13        GPC profile of agarose degraded by Agarase AS-II    95
| Figure 14        TLC profile of neoagarohexaose (N6) degraded by Agarase AS-II    96
| Figure 15        TLC profile of (N2 + N4) and neoagarobiose biosynthesized by 50 □L Agarase AS-II (0.018 U) at 45oC for 120 minutes    97
| Figure 16        HPLC profile of neoagarotetraose [retention time (RT) = 26.28 min] biosynthesized from neoagarobiose (RT = 28.20 min)    98
| Figure 17        TLC profile of an unidentified galactose oligomer (Rf = 0.60) biosynthesized from galactose (Rf = 0.67)    99
| Figure 18        HPLC profile of unidentified galactose oligomer (RT = 25.75 min) biosynthesized from galactose (RT = 27.74 min) for 2 hours    100
| Figure 19        HPLC profile of minor unidentified galactose polymer (RT = 21.34 min) and a major unidentified galactose polymer (RT = 25.83 min) biosynthesized from galactose (RT = 27.74 min) for 24 hours    101
| Figure 20        1H NMR spectrum of the unidentified galactose oligomer biosynthesized from galactose    102
| Figure 21        Changes of reducing sugar contents of 1% Gracilaria sp. or Monostroma nitidum extracted polysaccharides digested by 1.8 U/mL Agarase AS-II    103
| Figure 22        GPC profile of Gracilaria sp. extracted polysaccharides (Gra) with SephadexTM G-25 gels    104
| Figure 23        GPC profile of Gracilaria sp. extracted polysaccharides (Gra) with SephacrylR S-200 gels    105
| Figure 24        HPLC profile of Gracilaria sp. extracted polysaccharides (Gra)    106
| Figure 25        GPC profile of Gracilaria sp. extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Gra-C108) with SephadexTM G-25 gels    107
| Figure 26        GPC profile of Gracilaria sp. extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Gra-C108) with SephacrylR S-200 gels    108
| Figure 27        HPLC profile of Gracilaria sp. extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Gra-C108)    109
| Figure 28        GPC profile of Gracilaria sp. extracted polysaccharides digested by Agarase AS-II (Gra-AS-II) with SephadexTM G-25 gels    110
| Figure 29        GPC profile of Gracilaria sp. extracted polysaccharides digested by Agarase AS-II (Gra-AS-II) with SephacrylR S-200 gels    111
| Figure 30        HPLC profile of Gracilaria sp. extracted polysaccharides digested by Agarase AS-II (Gra-AS-II)        112
| Figure 31        GPC profile of M. nitidum extracted polysaccharides (Mon) with SephadexTM G-25 gels    113
| Figure 32        GPC profile M. nitidum extracted polysaccharides (Mon) with SephacrylR S-200 gels    114
| Figure 33        HPLC profile of M. nitidum extracted polysaccharides (Mon)    115
| Figure 34        GPC profile of M. nitidum extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Mon-C108) with SephadexTM G-25 gels    116
| Figure 35        GPC profile of M. nitidum extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Mon-C108) with SephacrylR S-200 gels    117
| Figure 36        HPLC profile of M. nitidum extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Mon-C108)    118
| Figure 37        GPC profile of M. nitidum extracted polysaccharides digested by Agarase AS-II (Mon-AS-II) with SephadexTM G-25 gels    119
| Figure 38        GPC profile of M. nitidum extracted polysaccharides digested by Agarase AS-II (Mon-AS-II) with SephacrylR S-200 gel    120
| Figure 39        HPLC profile of M. nitidum extracted polysaccharides digested by Agarase AS-II (Mon-AS-II)    121
| Figure 40        Maximum changes of viable bacterial counts of 2 mg/mL algal extracted polysaccharides or their agarase lysates fermented by 10% bifidobacteria within 24-hour incubation    122
| Figure 41        Maximum changes of pH of 2 mg/mL algal extracted polysaccharides or their agarase lysates fermented by 10% bifidobacteria within 24-hour incubation    123
| Figure 42        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of Gracilaria sp. extracted polysaccharides (Gra)    124
| Figure 43        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of Gracilaria sp. extracted polysaccharides digested by A. salmonicida MAEF108 crude agarases (Gra-C108)    125
| Figure 44        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of Gracilaria sp. extracted polysaccharides digested by Agarase AS-II (Gra-AS-II)        126
| Figure 45        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of M. nitidum extracted polysaccharides (Mon)    127
| Figure 46        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of M. nitidum digested by A. salmonicida MAEF108 crude agarases (Mon-C108)    128
| Figure 47        Cell viability of different cell density of Mesocricetus auratus kidney cells, BHK-21, affected by concentrations of M. nitidum extracted polysaccharides digested by Agarase AS-II (Mon-AS-II)    129
| Figure 48        Prevention abilities of algal extracted polysaccharides or their agarase lysates to against JEV infection to BHK-21 cells    130
|
| List of Appendix
|
| Appendix 1    Ion-exchange chromatography of Aeromonas salmonicida MAEF108 crude agarases    131
| Appendix 2    Calibration curve of the wide range marker (S-8445, Sigma) in 12% SDS-PAGE    132
| Appendix 3    First and second residues of Agarase AS-II analyzed by Edman degradation in N-terminal sequencing monitored via HPLC    133
| Appendix 3    (continued) Third and fourth residues of Agarase AS-II analyzed by Edman degradation in N-terminal sequencing monitored via HPLC    134
| Appendix 3    (continued) Fifth and sixth residues of Agarase AS-II analyzed by Edman degradation in N-terminal sequencing monitored via HPLC    135
| Appendix 4    Internal amino acid sequence via LC-MS/MS of Agarase AS-II that hit best alpha-agarase precursor of Alteromonas agarilytica    136
| Appendix 5        HPLC profile of neoagarotetraose (RT = 26.32 min) and neoagarobiose (RT = 28.16 min)    137
| Appendix 6    HPLC profile of neoagarohexaose (RT = 25.06 min)    138
| Appendix 7    Reducing sugar content standard curve    139
| Appendix 8    1H NMR spectrum of galactose    140
|
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