The synthesis and utilization of Cibachron Blue-amylose: A new chromogenic substrate for determination of amylase activity

Klein, Bernard; Foreman, James A.; Searcy, Ronald L.

doi:10.1016/0003-2697(69)90283-8

Cited by 52 publications

(7 citation statements)

References 11 publications

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“…Spores from the transformants were spread on solid defined agar to obtain separate colonies. This minimal agar consisted of a basal layer (20 ml) of minimal agar (Hopwood et al, 1985) containing 1 % glucose, 0n25 % (w\v) Casamino acids and G418 (15 µg ml − ") to maintain selective pressure for the presence of Tn5096, and a top layer (5 ml) of the same medium containing 2 % (w\v) Cibachron blue starch (CBS), as a chromogenic substrate for α-amylase (Klein et al, 1969). These cultures, called ' CBS plates ', were incubated for 3 d at 30 mC (no haloes were seen), then for 2-3 weeks at 40 mC.…”

Section: Methodsmentioning

confidence: 99%

Disruption of sblA in Streptomyces lividans permits expression of a heterologous α-amylase gene in the presence of glucose The EMBL accession number for the sequence reported in this paper is AJ223365.

et al. 1999

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In a transposition mutant of Streptomyces lividans TK24, the usually glucoserepressible expression of a heterologous α-amylase gene (aml) became resistant to glucose repression. The transposon had inserted into an ORF called sblA which encodes a 274 aa product sharing significant sequence similarities with various phosphatases that act on small phosphorylated substrates. sblA was transcribed as a monocistronic mRNA and its transcription was enhanced at the transition phase. Because its transcriptional and putative translational start points coincide, sblA is likely to be translated in the absence of a conventional RBS. The sblA-disrupted mutant is characterized by early growth arrest in glucose-grown cultures and by partial relief of glucose repression of aml expression.

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Section: Methodsmentioning

confidence: 99%

Disruption of sblA in Streptomyces lividans permits expression of a heterologous α-amylase gene in the presence of glucose The EMBL accession number for the sequence reported in this paper is AJ223365.

et al. 1999

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“…A consequence of this behavior is a colorless halo surrounding the amylolytic colonies as in the iodine method, but now bordered by a deep blue circle shaped by the di!using products [13,14]. The compounds resulting from blue starch hydrolysis di!use more rapidly in solid medium than non-hydrolyzed starch moieties.…”

Section: Introductionmentioning

confidence: 99%

A simple and rapid method for screening amylolytic bacteria

Effio

Silva

Pueyo

2000

Biochemical Education

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A laboratory class was designed for the study of the ecology of amylolytic bacteria in soil, although other sources may be equally suitable for this purpose. Groups of three students carried out the following: (a) preparation and sterilization of medium and plates, (b) collection and preparation of soil samples, spreading the samples on the plates, (c) incubation of the plates at 37 degrees C overnight, a further 1 h incubation at 60 degrees C to observe amylolytic activity due to thermophilic bacteria, and (d) interpretation and discussion of the results. These tasks are accomplished in two periods of 4h on consecutive days. No sophisticated instruments are required for these experiments, which can be carried out in three classes of 4h each. On the first day the students prepare culture media, buffers and reagents, as well as collect and grow soil samples. The second day is spent for both taxonomic identification of colonies and the HAI determination.

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“…These include starch coupled with Remazol brilliant blue (62, 113, 114); amylose linked to Cibachron blue (81,82,127); a cross-linked starch derivative coloured by a dye marker and given the commercial trade name 'Phadebas' (35,74,120);amylopectin dyed with Reactone red 2B (13,14,40,97,143); and amylopectin bound to Procion brilliant red M-2BS (116). In all the above methods, hydroly sis of the substrate leads to the liberation of water-soluble fragments contain ing the dye.…”

Section: Methodsmentioning

confidence: 99%

Amylase, Isoamylase and Macroamylase

Goldberg¹,

Spooner²

1975

Digestion

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Hyperamylasaemia has long been regarded as pathognomonic of acute pancreatitis. However, recent work has revealed a number of conditions where a gross elevation may be an incidental finding, notably diabetic ketoacidosis. The recent discovery of ‘macroamylase’, a high molecular weight amylase-protein complex capable of producing hyperamylasaemia with low urine amylase, has further complicated diagnosis and has led to the introduction of the ratio of amylase clearance to creatinine clearance as a diagnostic aid. Serum amylase may be resolved, by most electrophoretic media, into bands which correspond to those obtained when pancreatic homogenates or saliva are electrophoresed. The initial promise of this technique has not been realised at the routine diagnostic level. Duodenal juice amylase has been the classical enzyme used in assessing exocrine pancreatic function and although it is still of value it is being amplified by other enzyme tests.

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The synthesis and utilization of Cibachron Blue-amylose: A new chromogenic substrate for determination of amylase activity

Cited by 52 publications

References 11 publications

Disruption of sblA in Streptomyces lividans permits expression of a heterologous α-amylase gene in the presence of glucose The EMBL accession number for the sequence reported in this paper is AJ223365.

Disruption of sblA in Streptomyces lividans permits expression of a heterologous α-amylase gene in the presence of glucose The EMBL accession number for the sequence reported in this paper is AJ223365.

A simple and rapid method for screening amylolytic bacteria

Amylase, Isoamylase and Macroamylase

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