Purification and Characterization of Poly(γ-glutamic acid) Hydrolase from a Filamentous Fungus,Myrotheciumsp. TM-4222

1993 ◽  
Vol 57 (12) ◽  
pp. 2148-2153 ◽  
Author(s):  
Toshio Tanaka ◽  
Osamu Hiruta ◽  
Takafumi Futamura ◽  
Kazumichi Uotani ◽  
Atsuyuki Satoh ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Filamentous Fungus ◽  
Acid Hydrolase ◽  
Purification And Characterization

Purification and characterization of a cis-epoxysuccinic acid hydrolase from Bordetella sp. strain 1–3

2010 ◽  
Vol 69 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Xia Li ◽  
Tongcheng Xu ◽  
Hongbo Lu ◽  
Xiaohang Ma ◽  
Lei Kai ◽  
...  
Keyword(s):  
Acid Hydrolase ◽  
Purification And Characterization

Purification and characterization of glutamic acid dehydrogenase and α-ketoglutaric acid reductase from Peptococcus aerogenes

1972 ◽  
Vol 18 (6) ◽  
pp. 881-892 ◽  
Author(s):  
W. M. Johnson ◽  
D. W. S. Westlake
Keyword(s):  
Glutamic Acid ◽  
Kinetic Data ◽  
Acid Metabolism ◽  
The Other ◽  
Keto Acid ◽  
Glutamate Metabolism ◽  
Purification And Characterization ◽  
Acid Dehydrogenase ◽  
Acid Reduction

Two NAD-dependent enzymes involved in glutamic acid metabolism have been isolated from cell-free extracts of P. aerogenes. One enzyme, glutamic acid dehydrogenase, was shown to oxidatively deaminate glutamic acid yielding α-ketoglutaric acid in the presence of NAD but not NADP. The other enzyme, an NADH-requiring α-ketoglutarate reductase, reduced the α-keto acid to α-hydroxy-glutarate. The two NAD-dependent enzymes were separated, purified, and characterized. The results indicate that glutamic acid dehydrogenase, an enzyme not frequently implicated in anaerobic glutamate metabolism, is a predominating protein in extracts of P. aerogenes grown in the presence of glutamate. Kinetic data showed that the equilibrium of the latter reaction favored the direction of keto acid reduction.

Purification and Characterization of Poly(aspartic acid) Hydrolase fromSphingomonassp. KT-1

2001 ◽  
Vol 2 (4) ◽  
pp. 1155-1160 ◽  
Author(s):  
Kenji Tabata ◽  
Mariko Kajiyama ◽  
Tomohiro Hiraishi ◽  
Hideki Abe ◽  
Ichiro Yamato ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Acid Hydrolase ◽  
Purification And Characterization

scholarly journals Purification and characterization of an extracellular (1 → 6)-β-glucanase from the filamentous fungus Acremonium persicinum

1996 ◽  
Vol 316 (3) ◽  
pp. 841-846 ◽  
Author(s):  
Stuart M. PITSON ◽  
Robert J. SEVIOUR ◽  
Barbara M. McDOUGALL ◽  
Bruce A. STONE ◽  
Maruse SADEK
Keyword(s):  
Molecular Mass ◽  
Filamentous Fungus ◽  
Gel Filtration ◽  
Purification And Characterization ◽  
Eisenia Bicyclis ◽  
Ph Optimum ◽  
Hydrolysis Products ◽  
Sds Page ◽  
Hydrolysis Of

An endo-(1 → 6)-β-glucanase has been isolated from the culture filtrates of the filamentous fungus Acremonium persicinum and purified by (NH4)2SO4 precipitation followed by anion-exchange and gel-filtration chromatography. SDS/PAGE of the purified enzyme gave a single band with an apparent molecular mass of 42.7 kDa. The enzyme is a non-glycosylated, monomeric protein with a pI of 4.9 and pH optimum of 5.0. It hydrolysed (1 → 6)-β-glucans (pustulan and lutean), initially yielding a series of (1 → 6)-β-linked oligoglucosides, consistent with endo-hydrolytic action. Final hydrolysis products from these substrates were gentiobiose and gentiotriose, with all products released as β-anomers, indicating that the enzyme acts with retention of configuration. The purified enzyme also hydrolysed Eisenia bicyclis laminarin, liberating glucose, gentiobiose, and a range of larger oligoglucosides, through the apparent hydrolysis of (1 → 6)-β- and some (1 → 3)-β-linkages in this substrate. Km values for pustulan, lutean and laminarin were 1.28, 1.38, and 1.67 mg/ml respectively. The enzyme was inhibited by N-acetylimidazole, N-bromosuccinimide, dicyclohexylcarbodi-imide, Woodward's Regent K, 2-hydroxy-5-nitrobenzyl bromide, KMnO4 and some metal ions, whereas D-glucono-1,5-lactone and EDTA had no effect.

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