Application of cross-linked carboxymethyl cellulose degradation by beta-glucosidase and vaginal microbes to toxic shock syndrome.
نویسندگان
چکیده
Eleven bacterial and two yeast strains, four of which were previously identified as having activity on a lightly cross-linked carboxymethyl cellulose (CLD-2) found in one type of superabsorbent tampon, were grown on a variety of substrates, most containing cellulosics. None produced detectable amounts of cellulases, but all elaborated beta-glucosidase. None of these 13 strains nor 3 commercially obtained beta-glucosidase preparations could hydrolyze CLD-2, although a commercial cellulase and two other bacterial preparations known to produce cellulases could. Based on these results, it appears that previous work suggesting that the degradation of CLD-2 by vaginal microbes and beta-glucosidase is implicated in the production by Staphylococcus aureus of toxin causing toxic shock syndrome must be reevaluated.
منابع مشابه
Substrate specificity and mode of action of the cellulases from the thermophilic fungus Thermoascus aurantiacus.
The substrate specificities of three cellulases and a beta-glucosidase purified from Thermoascus aurantiacus were examined. All three cellulases partially degraded native cellulose. Cellulase I, but not cellulase II and cellulase III, readily hydrolyzed the mixed beta-1,3; beta-1,6-polysaccharides such as carboxymethyl-pachyman, yeast glucan and laminarin. Both cellulase I and the beta-glucosid...
متن کاملThe structural and functional contributions of β-glucosidase-producing microbial communities to cellulose degradation in composting
Background Compost habitats sustain a vast ensemble of microbes that engender the degradation of cellulose, which is an important part of global carbon cycle. β-Glucosidase is the rate-limiting enzyme of degradation of cellulose. Thus, analysis of regulation of β-glucosidase gene expression in composting is beneficial to a better understanding of cellulose degradation mechanism. Genetic diversi...
متن کاملCellulolytic Enzyme System of Thermoactinomyces sp. Grown on Microcrystalline Cellulose.
The carboxymethyl-cellulase and Avicelase activities of Thermoactinomyces sp., strain YX, were produced simultaneously with cell growth. Throughout the growth phase these activities were primarily extracellular, with up to 50% adsorbed to residual cellulosic substrate at any one time. On the other hand, the beta-glucosidase activity was associated with the culture solids throughout the entire f...
متن کاملProduction and Characterization of Highly Thermostable β-Glucosidase during the Biodegradation of Methyl Cellulose by Fusarium oxysporum
Production of β-glucosidase from Fusarium oxysporum was investigated during degradation of some cellulosic substrates (Avicel, α-cellulose, carboxymethyl cellulose (CMC), and methylcellulose). Optimized production of β-glucosidase using the cellulosic substrate that supported highest yield of enzyme was examined over 192 h fermentation period and varied pH of 3.0-11.0. The β-glucosidase produce...
متن کاملSynthesis and Characterization of Carboxymethyl Cellulose/Polystyrene Core-Shell Nanoparticles by Miniemulsion Polymerization
The first stage to have access to a reservoir is the drilling operation. The proper development of this operation plays a major role in increasing productivity. It must be pointed out that the drilling fluid (mud) is pivotal in achieving this objective. Among these fluids, water-based fluids are the most common ones, which have been utilized to drill approximately 80% of all wells and are m...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 50 3 شماره
صفحات -
تاریخ انتشار 1985