scholarly journals Purification and characterization of Bacillus coagulans oligo-1,6-glucosidase

1986 ◽  
Vol 158 (1) ◽  
pp. 77-83 ◽  
Author(s):  
Yuzuru SUZUKI ◽  
Yoshihiro TOMURA
Keyword(s):  
Bacillus Coagulans ◽  
Purification And Characterization

Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3

2005 ◽  
Vol 41 (1) ◽  
pp. 38-44 ◽  
Author(s):  
Satyendra Kumar ◽  
Khyodano Kikon ◽  
Ashutosh Upadhyay ◽  
Shamsher S. Kanwar ◽  
Reena Gupta
Keyword(s):  
Bacillus Coagulans ◽  
Purification And Characterization ◽  
Alkaliphilic Bacillus

scholarly journals Purification and characterization of thermo-alkaline stable lipase from Bacillus coagulans and its compatibility with commercially available detergents

2021 ◽  
Vol 26 (5) ◽  
pp. 2994-3001
Author(s):  
ABDULLAH A. AL-GHANAYEM ◽  
Keyword(s):  
Growth Parameters ◽  
Bacillus Coagulans ◽  
Iodoacetic Acid ◽  
Inhibitory Effect ◽  
Lipase Production ◽  
Maximum Activity ◽  
Purification And Characterization ◽  
Wide Range ◽  
Rrna Sequencing

Thermo-alkaline stable lipase producing B. coagulans was isolated and identified by 16S rRNA sequencing. The lipase production was optimized using different growth parameters. The enzyme was purified and characterized in terms of pH, temperature, solvents, heavy metal ions and inhibitors. Compatibility with commercially available detergents was also studied. The isolate showed maximum lipase production at 37 ⁰C; pH of 9 within 48 h. Addition of magnesium chloride increased lipase production. Sephadex G-100 chromatography was used to purify lipase. The enzyme showed maximum activity at pH 8 of 30 ⁰C. Lipase form B. coagulans was active at a wide range of temperature between 30-70 ⁰C. It was stable in most of the solvents at a concentration 5 and 10%, except dimethyl sulfoxide (DMSO) and methanol. Iodoacetic acid (IAA) and p-chloromercuribenzoic acid (pCMB) had an inhibitory effect on lipase. The lipase was compatible with commercially available detergents that increased the brightness and whiteness of the tested cotton fabrics. Lipase from B. coagulans with alkaline stability at a wide range of temperature has potential application in the detergent industry.

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

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