𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Purification and properties of the β-glucosidase from a nitrile hydratase-producing Brevibacterium sp. strain R312

✍ Scribed by J. L. Legras; M. R. Kaakeh; Dr. A. Arnaud; P. Galzy

Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
555 KB
Volume
29
Category
Article
ISSN
0233-111X

No coin nor oath required. For personal study only.

✦ Synopsis

Besides its nitrile hydratase and wide spectrum amidase activities, the Brevibacterium sp. R312 strain also possesses a constitutive beta-glucosidase. Its optimum pH is 6. The enzyme was purified by fractionation precipitation with ammonium sulfate followed by chromatographic elutions on Q-Sepharose Fast Flow, Sephadex G-200 and Phenyl Superose. The resulting purification was 1960 folds for a 6% yield. The molecular weight of this enzyme was estimated at 180,000. It contains two identical sub-units. The pI is 5.5. This enzyme has a strong affinity for aryl-beta-glycosides:pNPG, prunassine; it could also degrade linamarine. It is inhibited by p-chloromercuribenzoate, delta-gluconolactone and glucose.

📜 SIMILAR VOLUMES

The N-terminal amino acid sequences of B
The N-terminal amino acid sequences of Brevibacterium sp. R312 nitrile hydratase
✍ R. Duran; C. K. N. Chan Kwo Chion; F. Bigey; Prof. A. Arnaud; P. Galzy 📂 Article 📅 1992 🏛 John Wiley and Sons 🌐 English ⚖ 608 KB

## Abstract Nitrile hydratase from __Brevibacterium__ sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their N‐terminal amino acid sequences were found to be identical to those of __Rhodococcus__ sp. N‐774 nitri

Purification and characterization of nit
Purification and characterization of nitrile hydratase of a mutant strain of Brevibacterium sp.
✍ J. L. Moreau; S. Azza; Prof. Dr. A. Arnaud; P. Galzy 📂 Article 📅 1993 🏛 John Wiley and Sons 🌐 English ⚖ 429 KB

## Abstract The nitrile hydratase from the mutant strain of __Brevibacterium__ sp. ACV2 was purified and compared to that from the wild type R312. Its molecular weight was estimated at 80000. This enzyme is composed of 2 sub‐units with 26000 and 27500 molecular weights. The nitrile hydratase of the

Purification and properties of an acylam
Purification and properties of an acylamide amidohydrolase (E. C. 3.5.1.4) with a wide activity spectrum from Brevibacterium sp. R 312
✍ A. Thiery; M. Maestracci; Dr. A. Arnaud; P. Galzy; M. Nicolas 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 781 KB

An amidase with a wide activity spectrum was purified from the Brevibacterium sp. R 312 and studied. The purification was performed by precipitating the proteins of the supernatant fraction obtained after centrifugation of sonicated cells. The resulting proteins were submitted to a gel filtration st

Purification and properties of the β-glu
Purification and properties of the β-glucosidase of a new strain of Candida molischiana able to work at low pH values: Possible use in the liberation of bound terpenols
✍ Yann Vasserot; Patrick Chemardin; Prof. Dr. Alain Arnaud; Pierre Galzy 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 658 KB

A yeast strain isolated in the laboratory was studied and classified as a Candida molischiana. The P-glucosidase of this yeast strain was then purified. Its molecular weight, estimated by gel filtration, was 100,OOO. The enzyme consisted of only one subunit, identified after treatment with sodium do