Dissertations / Theses on the topic 'Xylanolytic and chitinolytic enzymes'
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McKenna, Ellen Margaret. "Xylanolytic enzymes of Ceraceomyces sublaevis." Thesis, University of Ulster, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.333973.
Full textO'Donnell, Raymond William. "Chitinolytic enzymes of Candida albicans." Thesis, University of Aberdeen, 1991. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=158392.
Full textManson, Forbes Donald Castell. "Chitinolytic enzymes of turbot, Scophthalmus maximus (L.)." Thesis, University of Aberdeen, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.277191.
Full textKellett, Louise Elizabeth. "The molecular biology of xylanolytic enzymes from Pseudomonas fluorescens subsp. cellulosa." Thesis, University of Newcastle Upon Tyne, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315636.
Full textOree, Glynis. "Chitin hydrolysis with chitinolytic enzymes for the production of chitooligomers with antimicrobial properties." Thesis, Rhodes University, 2019. http://hdl.handle.net/10962/67887.
Full textau, s. averis@murdoch edu, and Susana M. E. Severgnini. "Isolation and characterisation of two chitinase and one novel glucanase genes for engineering plant defence against fungal pathogens." Murdoch University, 2006. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20071213.105659.
Full textLeCleir, Gary R. "Chitinolytic bacteria and enzymes from Mono Lake, CA, USA." 2005. http://purl.galileo.usg.edu/uga%5Fetd/lecleir%5Fgary%5Fr%5F200512%5Fphd.
Full textDirected by James T. Hollibaugh. Includes an article published in Applied and environmental microbiology, and articles submitted to Aquatic microbial ecology, and Applied and environmental microbiology. Includes bibliographical references.
Chen, Chun-Jen, and 陳俊任. "Studies on Chitinolytic Enzymes from Aeromonas sp. No. 16." Thesis, 1993. http://ndltd.ncl.edu.tw/handle/24841666705890767379.
Full text國立臺灣大學
農業化學系
81
The partially hydrolyzed products of chitin and chitosan, N- acetylchitooligosaccharides and chitooligosaccharides, are of special interest because these oligosaccharides have been evalu- ated in various applications.This study focused on the production of N-acetylchitooligosaccharides by microbial enzymes. Crab shell chitin prepared by treating crab shell with acid and alkali was used as a substrate for isolating chitinolytic mi- croorganisms. Among the 103 isolated strains, strain No. 16 appeared to be the most potential chitinase-producing strain. It was identified belonging to the genus Aeromonas and named Aero- monas sp. No. 16. When the medium contained 1.5% colloidal chitin , 2.0% tryp- tone and 1.5% yeast extract with initial pH 10, Aeromonas sp. No. 16 could produce 1.4 units/milliliter of chitinase activity after 24 hours cultivation in 500 mL Hinton''''s flask. Using crys- talline chitin as substrate for enzyme productionin a 5L fermen- tor with temperature at 30℃, aeration at 1 vvm, agitation at 400 rpm and pH controlled between 7 and 8, chitinase activity could reach 1.5 units/milliliter after 30 hours cultivation. Chitin and N-acetylglucosamine were both found to be inducers for chitinase synthesis by Aeromonas sp. No. 16, on the other hand, addition of other carbohydrates would repress enzyme production with different degrees. Crude enzyme hydrolyzed chitin and produced N-acetylglucosa- mine as main product ,hydrolyzed chitosan with unknown products formation, which was supposed to be hetero- chitooligosaccharide. In crude enzyme, chitinase activity was most active at pH 6.0 and 50℃, and was stable at pH between 5 and 9 and at temperature be- low 40℃. β-N-acetyl-D- glucosaminidase was less stable at 40℃ and supposed to be an intracellular enzyme. After PAGE and acti-
Lin, Yuan-Ju, and 林芫如. "Study on Chitinolytic Enzymes from Serratia marcescens NTU-17." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/44846555575249611399.
Full text國立臺灣大學
生物產業機電工程學研究所
96
Abstract N-acetylchitooligosaccharides (degree of polymerization 4-6) have specific biological activities such as antitumor activity and immuno-enhancing effects. In this study, we aimed to isolate environmental microorganisms which could produce enzymes to hydrolyze chitin into N-acetylchitooligosaccharides. At the initial stage, we hydrolyzed colloidal chitin with crude microbial enzymes and analyzed the products by HPLC. From this screening, we found that the crude enzyme from one bacterial isolate could hydrolyze chitin and produce N-acetylchitooligosaccharides. The bacterial strain was identified by 16S rRNA sequencing and phylogenetic analysis to belong Serratia marcescens and was named S. marcescens NTU-17. We used central composite design (CCD) of response surface methodology (RSM) to obtain the optimal culture condition for chitinase production: 0.4 g/l colloidal chitin, 1.6 g/l casein, 30。C and pH 7.5; the highest chitinase activity was produced at 18 hours after inoculation. The crude enzyme from culture broth of S. marcescens NTU-17 was subjected to successive steps of purification. After ammonium sulfate fractionation (35-70%), gel filtration-Sephacryl 200 chromatography, and DEAE-Sephacel column chromatography, two species of chitinase were purified and the molecular weights were determined by SDS-PAGE to be 53 kDa (chitinase 1) and 39 kDa (chitinase 2). The chitinase activity of chitinase 1 and 2 were also verified by an in-gel chitinase activity assay. After purification, the specific activity of chitinase was increased by 2.5 fold and the yield was 12%. Chitinase 1 exhibited the optimal activity at pH 3 and 50℃, and chitinase 2 showed the optimal activity at 30℃ and similar activities at pH 3-12.
Wu, Li-Sen, and 吳立森. "Studies on chitinolytic enzymes from Aeromonas caviae No. 2." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/10837667822021624179.
Full text臺灣大學
微生物與生化學研究所
98
It was reported that N-acetylchitooligosaccharides (degree of polymerization 4-7) (GlcNAc)4-7 have specific biological activities such as antitumor activity and immuno-stimulating effects. In this study, we aimed to screen microorganisms from a chitin-rich environment and isolate the ones that can produce enzymes to hydrolyze chitin into N-acetylchitooligosaccharides. At the initial stage, we used the selection medium with colloidal chitin as the sole carbon source to select for microorganisms which could utilize chitin for growth. The microbial isolates were further screened by incubating the culture broth with colloidal chitin and analyzing the products by HPLC and TLC. Using this screening strategy, we obtained one bacterial isolate that could produce enzymes to hydrolyze chitin into (GlcNAc) 4-5 and hydrolyze chitosan into (GlcN/GlcNAc) 4-6. The bacterial strain was identified by 16S rDNA sequencing and phylogenetic classification to belong to Aeromonas caviae and was named Aeromonas caviae No. 2. To optimize the culture condition for producing higher amounts of chitinase, we first tested various culture pHs and temperatures and found that the highest chitinase activity was produced at pH 6 and 25℃. Using the central composite design (CCD) of response surface methodology (RSM), we further obtained the optimal concentrations of chitin and nitrogen sources in the culture medium to be colloidal chitin: 1.098%, soybean flour: 0.735% and yeast extract: 0.74%. The crude enzyme produced in selection medium went through successive steps of purification including ammonium sulfate precipitation (40-70%), chitin affinity-hydrolysis method and gel filtration chromatography (Sephacryl 200). After purification, four major proteins were found range from 55 to 100 kDa on the SDS-PAGE, and two of them showed chitinase activity range from 55 to 70 kDa on the in-gel chitinase activity assay. When proteins from the optimized culture medium were purified using nine major bands appeared range from 40 to 100 kDa on the SDS-PAGE, and three of them showed chitinase activity on the in-gel chitinase activity assay. Moreover, the purified proteins could hydrolyze chitin primarily into (GlcNAc)2 and hydrolyze chitosan into (GlcN/GlcNAc) 4-6.
Liao, Bei-Yu, and 廖倍瑜. "Studies on chitinolytic enzymes from a commercial crude papain prepartion." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/56933133869999033639.
Full text靜宜大學
食品營養研究所
92
Partially purified chitotriosidase and chitosanase were obtained from a commercial crude papain preparation using the sequential steps of buffer (containing 1.66 mM pHMB) extraction, 70% saturation ammonium sulfate precipitation and Sephacryl S-100 gel filtration. For hydrolysis of chitotriose derivative 4-methylumbelliferyl-β-D-N,N’,N” triacetylchitotriose (4-MU-β-GlcNAc3), the partially purified chitotriosidase had an optimal pH of 4.0, an optimal temperature of 40~50℃, a Km of 9.33μM and a Vmax of 0.476 nmol/min/mg. For hydrolysis of p-nitrophenyl-β-D-N-acetyl-glucosamine oligomer (pNP-β-GlcNAc1-5), the enzyme had much higher activity toward pNP-β-GlcNAc than toward other p-nitrophenyl-β-D-N-acetylglucosamine oligomers for release of p-nitrophenol. This suggests that the partially purified enzyme contained exo-type β-N-acetylglucosaminidase activity. In addition to pNP-β-GlcNAc hydrolysis activity, the enzyme also showed activity toward pNP-β-(GlcNAc)3-5 oligomer. The rate of the reaction was observed in the following order, pNP-β-(GlcNAc)4>pNP-β-(GlcNAc)3>pNP-β(GlcNAc)5. However, the enzyme had no activity toward pNP-β-(GlcNAc)2. These results indicate that the partially enzyme contained endo-type chitotriosidase and the cleavage site of the chitotriosidase may be the third and fourth linkages from the non-reducing terminus of pNP-β-(GlcNAc)n. Partially purified chitosanase consisted of several isoforms of chitinase and chitosanase, as analyzed by native-PAGE (pH 4.3) and chitinase and chitosanase activity staining. For hydrolysis of ethylene glycol chitin, the enzyme had an optimal pH of 3.0, an optimal temperature of 60℃, a Km of 1.24 mg/mL and a Vmax of 263 nmol GlcNAc/min/mg. Relative rate for hydrolysis of colloidal chitin, CM-chitin and ethylene glycol chitin were 30, 40 and 100, respectively. After incubation at 70℃ for 1 hour, 86% of the chitinase activity still remained. For hydrolysis of chitosan, the enzyme had an optimal pH of 4.6, an optimal temperature of 70℃, a Km of 1.58 mg/mL and a Vmax of 61.35 nmol GlcN/min/mg. Relative rate for hydrolysis of glycol chitosan, fungial chitosan (MW 390 kDa), shrimp chitosan (MW 340 kDa), crab chitosan (MW 300 kDa) and crab chitosan (MW 1,100 kDa) were 5, 24, 53, 73 and 100, respectively. After incubation at 70℃for 1 hour, 75% of the chitosanase activity still remained. The main products of chitosan hydrolysis catalyzed by the enzyme were low molecular weight chitosan (48 kDa~1.7 kDa) and some chitooligosaccharides.
Chen, Jung-Long, and 陳政融. "Application of chitin particles on the purification of chitinolytic enzymes and proteases." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/66140102691115380399.
Full text淡江大學
化學學系碩士班
99
Application of NF and Crude SSC on the purification of enzymes to achieve rapid purification purposes. Adsorbent : SP, AC, pure chitin, Crude SSC, Crude CSC, Crude SPC , Choose a more suitable adsorbent Crude SSC. Studying temperature, weight, time on the adsorption effect of the pineapple enzyme. By experiment that at 4 ℃, 30 min, 0.1 g of the conditions to get specific activity 0.0918 U / mg. Studying temperature, weight, time on the effect of NF adsorption bromelain enzyme. Learned from the experiment at 25 ℃, 30 min, 0.1 g of the conditions to get specific activity 0.1357 U / mg. Use the above conditions, NF, and Crude SSC absorption bacterial enzyme purified enzyme to discuss the results. Purified enzyme affected by the experimental conditions known isoelectric point is not the only factor, but also need to consider the interaction between enzyme and adsorbents as well as physical absorption and other factors. Results show that absorption is a viable way to purify the enzymes, it can improve the purification efficiency.
Yi, Chun, and 廖純沂. "Plasma haptoglobin phenotypes and chitinolytic enzymes study and its clinical application in cardiovascular disease." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/26232093401404827863.
Full text中山醫學大學
醫學研究所
97
Backgrounds Little is known about the association between human haptoglobin phenotypes and diseases. Also, not much is known about the association between blood chitinolytic enzyme levels and human diseases. Recent studies have suggested a link between haptoglobin and the molecules associated with inflammation. Subsequent discoveries on its roles in T-cell development and the governing signaling pathways have further enlightened both basic and epidermiological studies. The understanding of human chitinases, on the other hand, is relatively limited. To our knowledge, lacking of rapid and convenient analytical methods has limited the progress on studying both molecules in human. Our study aimed to develop rapid and accurate biochemical methods in analyzing (1) the haptoglobin phenotypes in human plasma, and (2) the specific activity of chitinolytic enzymes. These analytical methods were then applied to plasma samples from clinical and general populations in investigating the possible associations between human diseases and these traits. Methods We have developed a new method, termed mCBB-R250 staining, for rapid and sensitive typing of haptoglobin phenotypes from human plasma. The percentage of frequencies and the proportion of the three haptoglobin phenotypes, Hp 1-1, Hp 2-1, and Hp 2-2, in our collection of human plasma samples were analyzed using descriptive statistic, one sample t test and Chi-square tests. Using glycol chitosan as substrate, an analysis method using (K3Fe(CN)6) as indicator were developed to determine the chitioson-degrading enzymes in human plasma. An in-gel activity staining method was also developed for the detection and separation of chitinolytic enzymes. The specific activities of chitinolytic enzymes were analyzed using the normality test, independent-sample parametrical test, or non-parametrical test. Results We have successfully applied the mCBB-R250 method to determine the Hp phenotypes of 1148 samples. Among these, 11.67% are Hp 1-1, 42.60% are Hp 2-1, and 45.73% are Hp 2-2 type. As a comparison, the distribution of the three Hp phenotypes, as determined for 151 plasma samples from patients with cardiovascular diseases, are 11.26%, 41.06%, and 47.68% respectively for Hp 1-1, 2-1, and 2-2 type. These percentages are similar to that of the general population. Among the 151 samples from cardiovascular disease patients, 101 are stable angina (CAD), and the rest 50 are acute coronary syndrome (ACS) patients. While the percentages of Hp 2-2 type are statistically indifferent between these groups, the percentages of the Hp 1-1 and Hp 2-1 types are significantly different among CAD and ACS groups, in which we found that Hp 2-1 type is higher in CAD, but Hp 1-1 is higher in ACS. Using glycol chitosan and (K3Fe(CN)6) solution, the specific activities of chitinoltic enzymes, after analyzing 899 human plasma samples, was determined to be a normal distribution, with an average specific activity of 92.00 U/mg (95% CI 90.584,93.416). We have found that, among 151 patients of cardiovascular diseases, the specific chitinolytic enzyme activities in CAD group (102.724 U/mg) are higher than those in the ACS group (90.513 U/mg). We have also developed an in-gel detection method for rapid separation and detection of chitinolytic enzymes. With this new method, we have identified a new chitinolytic enzyme with a molecular weight of about 30 kDa. Conclusion We have developed rapid, accurate, and inexpensive methods for haptoglobin phenotyping and chitinolytic enzyme activity staining. The methods were applied to the Hp phenotyping and chitinolytic enzyme activity detection of 1178 plasma samples. With their application in clinical studies, these methods may grant us further understandings on the possible association with human diseases.
Chen, Chung-Chih, and 陳重志. "Studies on the production of chitinolytic enzymes and other antioxidants from Bacillus cereus TKU006." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/90055006557117072365.
Full text淡江大學
生命科學研究所碩士班
97
The purpose of this thesis is to study the production of chitinolytic enzymes and other antioxidants from Bacillus cereus TKU006. The optimum culture conditions for chitosanase and other antioxidants production were composed of 1% squid pen powder, 0.1% K2HPO4, 0.05% MgSO4.7H2O shaken at 25℃ in 100 mL of liquid medium in an Erlenmeyer flask (250 mL) for 3 days and 25 mL of liquid medium for 2 days, respectively. The optimum culture carbon/nitrogen source for chitinase production was 2% shrimp head powder incubated for 2 days. A chitinase and a chitosanase were purified by chromatography procedures of ion exchange and gel filtration. The molecular mass of the chitinase and chitosanase determined by SDS-PAGE were approximately 39 kDa and 44 kDa, respectively. The chitinase was completely inactivated by Fe2+, and the chitosanase was completely inactivated by Fe2+ and Cu2+. The optimum temperature, optimum pH, thermal stability and pH stability of chitinase were 60℃, pH 5, ≦50℃, pH 2-8 . The optimum temperature, optimum pH, thermal stability and pH stability of chitosanase were 60℃, pH 7, ≦50℃, pH 3-10. After squid pen powder fermented, the antioxidant properties by the assays of radical scavenging, metal chelating, reducing power and total phenolic content were reached at 75%, 97%, 441 μg/mL cysteine equivalent and 815 μg/mL gallic acid equivalent, respectively. Correlation between DPPH scavenging ability and total phenolic content were r=0.92.
高逸馨. "Isolation and identification of chitinolytic bacteria in human feces and purification of the hrolytic enzymes." Thesis, 2002. http://ndltd.ncl.edu.tw/handle/79609331051286195613.
Full textZhang, Meng. "The chitinolytic enzyme system of the compost-dwelling thermophilic fungus Thermomyces lanuginosus." Thesis, 2014. http://hdl.handle.net/10321/1698.
Full textChitin, a highly insoluble 1,4- -linked polymer of N-acetyl- -D-glucosamine, is the second-most abundant bio-polysaccharide in nature after cellulose. Most chitinolytic fungi are known to produce more than one kind of chitinase. The recent sequencing of the Thermomyces lanuginosus SSBP genome by our group has revealed four putative family 18 chitinases. In this study, three novel chitinase genes (chitl, chit2 and chit3) and the previously reported chit4 gene were cloned from Thermomyces lanuginosus SSBP and their gene structures were analysed. chit3, encoding a 36.6 kDa protein, and chit4, encoding a 44.1 kDa protein, were successfully expressed in Pichia pastoris. The recombinant Chit3 and Chit4 enzymes exhibited optimum activity at pH 4.0 and 5.0 and at 40oC and 50°C, respectively. Chit3 was stable at 40oC and retained 71% of its activity at 50°C after 60 min, while Chit4 was stable at 50°C and retained 56% of its activity at 60°C after 30 min. Both enzymes produced chitobiose as the major product using colloidal chitin, chitooligosaccharides and shrimp shell powder as substrates. Of the fungal strains tested, Chit3 displayed antifungal activity against Penicillium sp. and Aspergillus sp. This is the first report on the multi-chitinolytic system of T. lanuginosus and enzyme characterization has shown the potential of the enzymes to be used in degradation of the under-utilized bio-resource chitin.
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