Esculin hydrolysis reaction by Escherichia coli.

نویسندگان

  • A Miskin
  • S C Edberg
چکیده

The literature contains variable reports concerning the hydrolysis of esculin by members of the family Enterobacteriaceae and particularly Escherichia coli. We examined 113 strains of fresh clinical isolates of E. coli and assessed the ability of colonies in a population to hydrolyze esculin with and without preincubation in inducible substrates at 24, 48, and 72 h. The number of strains capable of fermenting salicin, a sugar with a beta-glucoside linkage like esculin, was studied under the same conditions. A strip test that measured the presence of the constitutive glucosidase was also performed with and without preincubation in inducible substrates. No E. coli strain was able to produce constitutive enzyme; preincubation in esculin and salicin resulted in an induction of the beta-glucosidase. The number of colonies able to hydrolyze esculin increased with time. Only those strains preincubated in esculin or salicin were able to produce a positive constitutive strip test. Because the beta-glucosidase of E. coli is inducible, one should employe, when using growth media, a light inoculum obtained by touching the top of a colony with a bacteriological wire and read the reaction between 18 and 24 h, or perform a rapid strip or spot test.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Esculin hydrolysis by Enterobacteriaceae.

Literature reports disagree concerning esculin hydrolysis in the family Enterobacteriaceae. A total of 2,490 strains of the family were investigated for esculin hydrolysis by two methods, the esculin spot test and the PathoTec incubation strip, which measures constitutive enzyme, and five growth-supporting methods, which determine both constitutive and inducible enzymes. The five growth-support...

متن کامل

Detection of the eaeA Gene in Escherichia coli Isolated from Broiler Chickens by Polymerase Chain Reaction

The aim of this study was to isolate Escherichia coli from chickens and to determine the presence of the eaeA gene, a virulence factor detected in Escherichia coli, in the isolates by polymerase chain reaction (PCR). Different chicken organs (lung, liver and spleen) were inoculated onto blood agar and biochemical tests were performed on the suspicious isolates. Escherichiacoliwas isolated from ...

متن کامل

Rapid test for determination of esculin hydrolysis.

An esculin hydrolysis test is described which distinguishes over 97% of bacteria that can convert esculin to esculetin in a buffered solution, from those that cannot, within an hour.

متن کامل

Characterization of β-Lactamases from Urinary Isolates of Escherichia coli in Tehran

Knowledge of antimicrobial resistance patterns in E. coli, the predominant pathogen associated with urinary tract infections (UTI) is important as a guide in selecting empirical antimicrobial therapy. Methods: To describe the antimicrobial susceptibility of E. coli associated with UTI in a major university hospital in Tehran (Iran), seventy-six clinical isolates of E. coli were studied for susc...

متن کامل

Identification and purification of a protein that stimulates the helicase activity of the Escherichia coli Rep protein.

A polypeptide (Mr = 15,000) has been purified from Escherichia coli cell extracts that significantly stimulates the duplex DNA unwinding reaction catalyzed by E. coli Rep protein. The Rep helicase unwinding reaction was stimulated by as much as 20-fold, upon addition of the stimulatory protein, using either a 71-base pair or a 343-base pair partial duplex DNA molecule as a substrate. The purifi...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of clinical microbiology

دوره 7 3  شماره 

صفحات  -

تاریخ انتشار 1978