Purification and Properties of a Novel sp . R 48 Enzyme , Trehalose Synthase , from Pimelobacter
نویسنده
چکیده
transglucosy]ation. The enzyme also converted trehatose into ma]tose but was inactive on o-ther saccharides. The N-termina] amino acid of the enzyme was serine. The optimum pH and temperature were pH 7.5 and 200C, respective]y, The enzyme was stab]e in the range of pH 6,O-9.0 and up to 30eC for 60 min. The rate of conyeTsion of maltose ;nto trehalose was independent of the mattose concentration. The maximum yietd of L'.e,hl.:OhSiebif:ti'MbyMca.tt,OS,r HWge:e, ,8k',/IX.': z80.',9.`{',..a:dTl 6,:7`Zi at 5. 15, and 250C, respectively. The hctivity
منابع مشابه
Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1
This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...
متن کاملPurification and Characterization of a Thermostable Neutrophilic Metalloprotease from Pseudomonas sp. DR89
A novel neutrophilic metalloprotease was isolated from Pseudomonas sp. DR89 isolate which was identified ina mineral spring in Iran. The enzyme was purified from the isolate to 21-folds in a three-step procedure involving ammonium sulfate precipitation, Q-Sepharose ionic exchange and Sephadex G-100 gel filtrationchromatography. Resuts showed that the enzyme was active at high temper...
متن کاملCloning and Characterization of the Gene for Amylosucrase from Neisseria polysaccharea: Production of a Linear a-1,4-Glucan
The gene for the amylosucrase from Neisseria polysaccharea (ATCC 43768) was cloned by use of a functional expression system in Escherichia coli XL1-Blue. The deduced amino acid sequence of the protein has homology to the sequences of the a-amylase class of enzymes, with the highest similarities being found to the sequences of the trehalose synthase from Pimelobacter sp. strain R48 (17) and amyl...
متن کاملA novel low molecular weight extracellular protease from a moderately halophilic bacterium Salinivibrio sp. strain MS-7: production and biochemical properties
Kinetics of bacterial growth and protease production were monitored on a novel isolated moderately halophilic bacterium, Salinivibrio sp. strain MS-7, and maximum growth and protease activity was achieved after 48 hours at 30°C and 180 rpm. To determine the effect of various carbon sources on protease production, glucose, lactose, sucrose and maltose were investigated and maximum production of...
متن کاملCloning and characterization of the gene for amylosucrase from Neisseria polysaccharea: production of a linear alpha-1,4-glucan.
The gene for the amylosucrase from Neisseria polysaccharea (ATCC 43768) was cloned by use of a functional expression system in Escherichia coli XL1-Blue. The deduced amino acid sequence of the protein has homology to the sequences of the alpha-amylase class of enzymes, with the highest similarities being found to the sequences of the trehalose synthase from Pimelobacter sp. strain R48 (17) and ...
متن کامل