諸如蝦頭、蝦殼、蟹殼、魷魚軟骨之類的含幾丁質水產副產物因於多種領域之應用價值而備受重視。Paenibacillus sp. TKU042 所生產幾丁聚醣酶、蛋白酶以及Paenibacillus sp. TKU047 所生產幾丁聚醣酶，於含魷魚軟骨(SPP)培養基可得最高產率，而P. mucilaginosus TKU032所生產幾丁聚醣酶以及Bacillus licheniformis TKU004所生產具葡萄糖苷酶抑制活性(AAG)之蛋白質(TKU004P)，則於含蝦頭粉(SHP)之培養基可得最高產率。針對上述所得產物進行分離，並且利用SDS-PAGE分析分子量結果，TKU004P分子量為29 kDa, Paenibacillus sp. TKU042 之幾丁聚醣酶及蛋白酶之分子量分別為70 kDa 及35 kDa。P. mulcilaginosus TKU032之幾丁聚醣酶之分子量為59 kDa, Panibacillus sp. TKU047 之幾丁聚醣酶之分子量為23 kDa。TKU004P 為具水解酵母菌AAG活性之一種蛋白酶。P. mucilaginosus TKU032及Paenibacillus sp. TKU032 所生產幾丁聚醣酶皆屬能用來生產幾丁聚寡醣(COS)之外切型幾丁聚醣酶。TKU032幾丁聚醣酶水解懸浮態幾丁聚醣所得三個COS區分當中，第一區分具有最高之葡萄糖苷酶抑制活性(65.86%, 20 mg/mL), 區分二和區分三則分別具有較強DPPH抗氧化活性, 分別為 79.00%, 12 mg/mL 以及 73.29%, 16 mg/mL。完全去乙醯幾丁聚醣經TKU047幾丁聚醣酶水解所得COS (GlcN)2-9 具有較市售COS更強之DPPH抗氧化活性。

Chitinous fishery by-products such as shrimp heads, shrimp shells, crab shells, squid pens are received great attention due to their applications in many fields. In this study, chitosanase, and protease from Paenibacillus sp. TKU042 and chitosanase from Paenibacillus sp. TKU047 possessed the highest productivity on squid pen powder (SPP), whereas a chitosanase from P. mucilaginosus TKU032 and a protein with anti-α-glucosidase (AAG) activity from Bacillus licheniformis TKU004 (TKU004P) were on shrimp head powder (SHP). The purification process was performed to obtain the purified proteins. Using SDS-PAGE analysis, the molecular weight of those enzymes and TKU004P was determined, for instance, TKU004P was 29 kDa, chitosanase and protease from Paenibacillus TKU042 were 70 kDa and 35 kDa (respectively), chitosanase from P. mucilaginosus TKU032 was 59 kDa, and chitosanase from Paenibacillus sp. TKU047 was 23 kDa.  TKU004P was then investigated as a protease and demonstrated AAG activity by degrading yeast α-glucosidase. Chitosanases from P. mucilaginosus TKU032 and Paenibacillus sp. TKU047 were investigated as the endochitosanases, which could be used to produce chitosan oligosaccharide (COS). Three COS fractions were obtained from hydrolyzed colloidal chitosan that was catalyzed by TKU032 chitosanase. Among them, fraction I showed the highest α-glucosidase inhibitor (aGI) activity (65.86% at 20 mg/mL), and fractions II and III exhibited strong 2,2-diphenyl1-picrylhydrazyl (DPPH) radical scavenging activity (79.00% at 12 mg/mL and 73.29% at 16 mg/mL, respectively). The COS obtained from the hydrolysis of fully deacetylated chitosan catalyzed by TKU047 chitosanase was (GlcN)2-9 and expressed a higher DPPH radical scavenging activity than that from the commercial COSs.

Acknowledgments	I
Abstract	II
Abbreviation Used	IV
Catalog	V
List of Figures	VIII
List of Tables	X
Introduction	1
Chapter 1. Conversion of Squid Pens to Chitosanases and Proteases via Paenibacillus sp. TKU042 	4
1.1. Introduction	4
1.2. Results and Discussion	6
1.2.1. Screening of Chitinous Materials as sole C/N for Chitosanase Production	6
1.2.2. Effect of SPP Concentration on Chitosanase, Protease and αGI Production	6
1.2.3. Production of Chitosanase, Protease and αGI from SPP and deCSP by Different Bacteria	7
1.2.4. Purification and Characterization of Chitosanase and Protease	10
1.3. Materials and Methods	12
1.3.1. Materials	12
1.3.2. Measurement of Enzyme Activities	13
1.3.3. Measurement of Alpha Glucosidase Inhibitor	13
1.3.4. Screening of Chitinous Materials as Sole C/N for Enzyme Activity	14
1.3.5. Effect of SPP Concentration on Enzymes and αGI Activity	14
1.3.6. Production of Enzymes and αGI from SPP and deCSP Using Different Bacteria	14
1.3.7. Purification of Chitosanase and Protease	15
1.4. Conclusions	15
Chapter 2. Anti-α-Glucosidase Activity by a Protease from Bacillus licheniformis	19
2.1. Introduction	19
2.2. Results and Discussion	20
2.2.1. Extraction of AAG Protein	20
2.2.2. AAG Mechanism	22
2.2.3. Proteolytic Activity	24
2.2.4. pH Stability of TKU004P	25
2.2.5. Utilization of C/N Source for TKU004P Production 	26
2.2.6. Effect of TKU004P on Different Enzymes	27
2.2.7. Comparison of AAG Activity by Different Proteases	27
2.3. Materials and Methods 	28
2.3.1. Materials	28
2.3.2. AAG Activity	29
2.3.3. Protease Activity Assay	29
2.3.4. Extraction of TKU004P	29
2.3.5. AAG Mechanism	30
2.3.6. Proteolytic Activity	30
2.3.7. pH Stability	30
2.3.8. Utilization of C/N Source for TKU004P Production	30
2.3.9. Effect of TKU004P on Different Enzymes	31
2.3.10. Comparison of AAG Activity by Different Proteases	31
2.4. Conclusions	31
Chapter 3. Production of a Thermostable Chitosanase from Shrimp Heads via Peanibacillus mucilaginosus TKU032 Conversion and its Application in the Preparation of Bioactive Chitosan Oligosaccharides	35
3.1. Introduction	35
3.2. Results and Discussion	36
3.2.1. Screening of Chitinous Materials as Sole C/N Source for Chitosanase Production	36
3.2.2. Comparison of Chitosanase Production from SHP using Different Bacteria	37
3.2.3. Purification and Characterization of Chitosanase	38
3.2.4. Effects of pH and Temperature on Activity and Stability of Chitosanase	39
3.2.5. Effect of Metal Ions on Activity of Chitosanase	40
3.2.6. Substrate Specificity of Chitosanase	41
3.2.7. COS Production	42
3.2.8. Evaluation of Antioxidant and aGI Activities of COS Fractions	43
3.3. Materials and Methods 	45
3.3.1. Materials	45
3.3.2. Measurement of chitosanase activity	45
3.3.3. Screening of Chitinous Materials as Sole C/N Source for Chitosanase Activity	45
3.3.4. Purification of Chitosanase	45
3.3.5. Effects of pH and Temperature on Activity and Stability of Chitosanase	46
3.3.6. Effect of Metal Ions on Chitosanase Activity	46
3.3.7. Substrate Specificity of Chitosanase	46
3.3.8. Antioxidant Activity Assay	46
3.3.9. αGI Activity Assay	46
3. 4. Conclusions	47
Chapter 4. Bioprocessing of Squid Pens Waste into Chitosanase by Paenibacillus sp. TKU047 and Its Application in Low-Molecular Weight Chitosan Oligosaccharides Production	52
4.1. Introduction	52
4.2. Results and Discussion	54
4.2.1. Screening of Suitable C/N Source for Chitosanase Production by Paenibacillus sp. TKU047	54
4.2.2. Isolation of Paenibacillus sp. TKU047 Chitosanase	56
4.2.3. Effects of Temperature and pH	58
4.2.4. Effects of Divalent Metal Ions, EDTA, and Surfactants	59
4.2.5. Substrate Specificity and Hydrolysis Products	60
4.2.6. Preparation of COS	62
4.2.7.  Antioxidant Activity of COS	63
4.3. Materials and Methods 	65
4.3.1. Materials	65
4.3.2. Chitosanase Assay	65
4.3.3. Screening of Suitable C/N Source for Chitosanase Production	66
4.3.4. Isolation of Paenibacillus sp. TKU047 Chitosanase	66
4.3.5. Effects of Temperature and pH	67
4.3.6. Effect of Divalent Metal Ions, Surfactants, and EDTA	67
4.3.7. Substrate Specificity and Hydrolysis Products	67
4.3.8. Preparation of COS	68
4.3.9. Antioxidant Activity Assay	68
4.4. Conclusions	68
Appendix	74
List of Figures
Figure 1.1. Effect of SPP concentration on the production of chitosanase, protease and αGI by Paenibacillus sp. TKU042.	7
Figure 1.2. Effect of combining SPP with deCSP on the production of chitosanase, protease and αGI by Paenibacillus sp. TKU042.	7
Figure 1.3. Elution profile of chitosanase and protease on Macro-Prep High S	11
Figure 1.4. SDS-PAGE analysis of the protease and chitosanase produced by TKU042.	12
Figure 2.1. Elution profile of TKU004P on Macro-Prep High S chromatography	21
Figure 2.2. Anti-α-glucosidase (AAG) activity of TKU004P and acarbose.	21
Figure 2.3. SDS-PAGE analysis of the protease produced by B. licheniformis TKU004	22
Figure 2.4. Lineweaver–Burk plot analysis of AAG by TKU004P	23
Figure 2.5. HPLC analysis of the time-course reaction of TKU004P and yeast α-glucosidase	23
Figure 2.6. Effect of pH on the stability of TKU004P	25
Figure 2.7. Effect of the C/N source on AAG (a), optical density (OD) (b) and protease activity production (c) of B. licheniformis TKU004	26
Figure 2.8. Effect of TKU004P on different enzymes.	27
Figure 3.1. Production of chitosanase by P. mulaginosus TKU032.	37
Figure 3.2. A typical elution profile of chitosanase on Macro-prep High S column	38
Figure 3.3. SDS-PAGE analysis of the chitosanase produced by TKU032.	39
Figure 3.4. Effect of pH (a) and temperature (b) on activity (●) and stability (□) of TKU032 chitosanase.	40
Figure 3.5. Substrate specificity of P. mucilaginosus TKU032 chitosanase	41
Figure 3.6. Flow chart for the isolation of COS produced by hydrolyzing chitosan with TKU032 chitosanase	42
Figure 3.7. HPLC profiles of chitosan oligosaccharide fractions. (A) references; (B) chitosan oligosaccharide fractions	43
Figure 3.8. (A) antioxidant and (B) aGI activities of COS fractions	44
Figure 3.9. Lineweaver-Burk plot analysis of aGI activity by COS fraction I	44
Figure 4.1. Screening of suitable C/N source for chitosanase production by Paenibacillus sp. TKU047	55
Figure 4.2. SDS-PAGE and zymogram profiles of Paenibacillus sp. TKU047 chitosanase.	57
Figure 4.3. Effects of temperature and pH on the activity and stability of Paenibacillus sp. TKU047 chitosanase	59
Figure 4.4. Effects of some chemicals on the activity of Paenibacillus sp. TKU047 chitosanase	60
Figure 4.5. Substrates specificity of Paenibacillus sp. TKU047 chitosanase (a) and TLC profile of hydrolysis products of fully deacetylated chitosan by the purified enzyme (b).	61
Figure 4.6. MALDI-TOF mass spectrometry profile of the COS prepared from the chitosan hydrolysis process catalyzed by Paenibacillus sp. TKU047 chitosanase	63
Figure 4.7. DPPH radical scavenging activity of some COSs	64
 
List of Tables
Table 1.1. Comparison of chitinolytic enzyme, protease and αGI production by various bacteria using deCSP as C/N source	8
Table 1.2. Comparison of chitinolytic enzyme, protease and αGI production by various bacteria using SPP as C/N source	9
Table 1.3. Purification of the chitosanase from Paenibacillus sp. TKU042	11
Table 1.4. Purification of the protease from Paenibacillus sp. TKU042	11
Table 2.1. Result of time-course reaction of TKU004P and yeast α-glucosidase.	24
Table 2.2. Substrate specificity of TKU004P	25
Table 2.3. Comparison of the AAG activity produced by various proteases	28
Table 3.1. Comparison of chitosanase, chitinase, and exochitinase production by different Paenibacillus and Bacillus strains	38
Table 3.2. Purification of chitosanase from P. mucilaginosus TKU032	39
Table 3.3. Effect of metal ions on the activity of chitosanase	41
Table 4.1. Purification of Paenibacillus sp. TKU047 chitosanase	56
Table 4.2. Comparison of chitinase/chitosanase produced by Paenibacillus strains	58
Table 4.3. The characteristics of COS, CCOS_1, and CCOS_2.	63
Table 4.4. The IC50 value of DPPH radical scavenging activity of some COSs	65

introduction
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Chapter 2
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Chapter 3
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Chapter 4
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[4]	Wang, S.L.; Liang, T.W. Microbial reclamation of squid pens and shrimp shells. Res. Chem. Intermed. 2017, 43, 3445.
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