نتایج جستجو برای: alkalophilic bacillus

تعداد نتایج: 56370  

Journal: :Journal of bacteriology 1982
M Kitada A A Guffanti T A Krulwich

The bioenergetic properties and viability of obligately alkalophilic Bacillus firmus RAB have been examined upon incubation in alkaline and neutral buffers in the presence or absence of added Na+. At pH 10.5, cells incubated in the absence of Na+ exhibited an immediate rise in cytoplasmic pH from less than 9.5 to 10.5, and they lost viability very rapidly. Viability experiments in the presence ...

Journal: :Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] 2016
Sheila Lorena de Araújo Coelho Valter Cruz Magalhães Phellippe Arthur Santos Marbach Marcia Luciana Cazetta

Cyclodextrin glycosyltransferase (CGTase) catalyzes the conversion of starch into non-reducing cyclic sugars, cyclodextrins, which have several industrial applications. This study aimed to establish optimal culture conditions for β-CGTase production by Bacillus sp. SM-02, isolated from soil of cassava industries waste water lake. The optimization was performed by Central Composite Design (CCD) ...

2012
Marlene M Martínez Mora Karel Hernández Sánchez Reynaldo Villalonga Santana Arley Pérez Rojas Héctor L Ramírez Juan José Torres-Labandeira

Cyclodextrin glucanotransferase (CGTase, EC 2.4.1.9) is an unique enzyme capable of converting starch and related substrates into cyclodextrins (CDs). In this paper, we report an one step gel purification method of CGTase from Bacillus sp. and later enzyme characterization. The Bacillus sp. strain was isolated from a Colocacia esculenta rizospheric soil sample and the CGTase production was carr...

Journal: :Applied and environmental microbiology 1996
S F Lin C M Chiou C M Yeh Y C Tsai

An extracellular alkaline lipase of alkalophilic Pseudomonas pseudoalcaligenes F-111 was purified to homogeneity. The apparent molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 32,000, and the isoelectric point was 7.3. With p-nitrophenyl esters as its substrates, the enzyme shows preference for C12 acyl and C14 acyl groups. It was stable in the pH ran...

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