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1.
Anne M. Gallagher Catherine T. Kelly William M. Fogarty 《Applied microbiology and biotechnology》1991,35(4):455-460
Summary The ascosporogenous yeast Lipomyces tetrasporus produced an unusual extracellular carbohydrase. It was purified to homogeneity using ammonium sulphate precipitation and DEAE Bio-gel A ion-exchange chromatography. While retaining highest activity on low-molecular-weight saccharides such as maltose and nigerose, it displays considerable activity towards polymeric substrates including soluble starch. It is particularly unusual in that it also hydrolyses dextran and has a very high affinity for this substrate. The enzyme has an exo-lytic mode of action with the only hydrolysis product, glucose, being released in the -anomeric form. Optimum activity occurs at pH 4.5 and at 50°C. It is a glycoprotein, and has an M
r value of 150 000 (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) — 183 000 (fast protein liquid chromatography) and a pI of 6.0.
Offprint requests to: C. T. Kelly 相似文献
2.
Andrew M. Fogarty Olli H. Tuovinen 《Journal of industrial microbiology & biotechnology》1995,14(5):365-370
Summary
Pseudomonas paucimobilis was isolated from a consortium which was capable of degrading dicamba (3,6-dichloro-2-methoxybenzoic acid) as the sole source of carbon. The degradation of dicamba byP. paucimobilis and the consortium was examined over a range of substrate concentration, temperature, and pH. In the concentration range of 100–2000 mg dicamba L–1 (0.5–9.0 mM), the degradation was accompanied by a stoichiometric release of 2 mol of Cl– per mol of dicamba degraded. The cultures had an optimum pH 6.5–7.0 for dicamba degradation. Growth studies at 10°C, 20°C, and 30°C yielded activation energy values in the range of 19–36 kcal mol–1 and an average Q10 value of 4.0. Compared with the pure cultureP. paucimobilis, the consortium was more active at the lower temperature. 相似文献
3.
Bacillus sphaericus ATCC 7055 produced an intracellular cyclodextrinase (EC 3.2.1.54). It was purified by solublilising with Triton X-100, Q-Sepharose ion-exchange chromatography, phenyl-Sepharose CL-4B hydrophobic interaction chromatography and Superose-12 gel filtration and gave a single band on SDS-PAGE and preparative isoelectric focusing. The maxima for pH and temperature of the purified enzyme were pH 6.0–6.5 and 40°C. The enzyme had a relative molecular mass of 91 200–95 000 and an isoelectric point of 5.3. The amino-linked pseudotetrasaccharide, acarbose, inhibited activity. As well as cyclodextrins the enzyme was active on a broad range of substrates ranging in size from maltooligosaccharides (G3) to polysaccharides such as starch and pullulan, and branched cyclodextrins. End-product profiles of the cyclodextrinase on various substrates revealed that, upon hydrolysis of 1% (w/v) -, - and -cyclodextrin and maltoheptaose, glucose and maltose were the dominant end-products. Pullulan degradation resulted in panose (92%, w/v) as the main end-product, and glucose (27%, w/v) and maltose (37%, w/v) were the sole products formed from starch degradation. 相似文献
4.
Miniature "soft gel" filled breast prostheses were implanted into rats, and half of these were purposefully ruptured upon insertion. At sacrifice of the animals later, the position of the exuded gel, the variability of the capsule thickness, and the extent of the capsule formation were evaluated. The capsule thickness was significantly increased around the ruptured prostheses, in response to the exuded gel. Also, the gel migrated through the fibrous capsule and into the surrounding tissue, eliciting an inflammatory response there to produce capsule thickening. 相似文献
5.
Vitellogenin and vitellin of Manduca sexta and some other insect species were purified by immobilized metal ion affinity chromatography. Ferric ion was chosen as the immobilized metal ion. Agarose-bound carboxymethylpicolylamine was used as the chelating adsorbent for the ferric ion. Vitellogenin and vitellin, both phosphorylated lipoproteins, were shown to bind specifically to the iron. The general applicability of immobilized ferric ion affinity chromatography for the purification of insect vitellogenin and vitellin is suggested. 相似文献
6.
7.
William M. Fogarty Marian P. Brosnan Evelyn M. Doyle Catherine T. Kelly 《Applied microbiology and biotechnology》1992,37(2):191-196
Summary Two strains (NCIB 11412 and NCIB 10814) of the thermophilic organism Bacillus stearothermophilus were found to produce complex carbohydrase systems. The enzyme activities in each system include -amylase as the major component, maltase, pullulanase, a minor amylase and cyclodextrinase. The latter three activities are produced in low yield in both strains. A crude enzyme preparation from each strain possessed maltogenic properties on hydrolysis of soluble starch. Following rigorous purification procedures, the purified major -amylase from either strain did not produce maltose as a major end-product of starch hydrolysis. However, a partially purified mixture of pullulanase, minor amylase and cyclodextrinase activities from NCIB 11412 and NCIB 10814 produced 56.4% and 62.0% maltose, respectively, from soluble starch. 相似文献
8.
Bacillus sp. RK9 was isolated from soil and produced a constitutive polygalacturonate lyase. Production of the enzyme required the presence of complex nitrogen (peptone and yeast extract). Highest activity was obtained with an initial pH of 9.7. The organism was alkalophilic. No growth occurred below pH 7.5. The enzyme was purified by salt precipitation and diethylaminoethyl (DEAE) cellulose ion-exchange chromatography. The pH optimum for activity was 10.0 in 0.01 M glycine-NaOH buffer. Calcium alone, of divalent cations, activated the enzyme by 2.9-fold. Complete inhibition of enzyme activity was achieved by 1 mM ethylenediaminetetraacetic acid (EDTA). Hydrolysis of substrate occurred in a random fashion and the enzyme was 50% more active towards acid soluble pectic acid (ASPA) than towards sodium polypectate. 相似文献
9.