Protease production by a thermophilic Bacillus species (P-001A) which degrades various kinds of fibrous proteins

Atalo, K.; Gashe, Berhanu A.

doi:10.1007/bf00131207

Cited by 79 publications

(38 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Dac.521 had a short stationary phase followed by a rapid decrease in OD,,, with a concurrent decrease in detectable acetonitrile-degrading activity, consistent with a reduction or cessation of expression of the relevant gene(s) and induction of a specific degradation pathway (Morihara, 1974;Atalo & Gashe, 1993).…”

Section: Growth and Activity Profilesmentioning

confidence: 81%

Novel thermophilic bacteria producing nitrile-degrading enzymes

1997

View full text Add to dashboard Cite

Summary: The first known report of the isolation of thermophilic bacteria which produce nitrile-degrading enzymes is presented. One of the strains isolated was studied in detail. Strain Dac521, classified as Bacillus pallidus, was capable of growth on acetonitrile, benzonitrile, propionitrile, acetamide, benzamide and propionamide as the sole carbon and nitrogen source in minimal nutrient media. The strain produced separate aliphatic-nitrile (e.g. acetonitrile)- and aromatic-nitrile (e.g. benzonitrile)-degrading activities. Acetonitrile-degrading activity was produced constitutively and enzyme production was not enhanced by the addition of substrate. Under conditions where benzonitrile was the sole carbon and nitrogen source in minimal nutrient media, acetonitrile-degrading enzyme activity was completely inhibited and benzonitrile-degrading activity was induced. Growth on substrates as sole carbon and nitrogen sources, together with the substrate specificity of cell-free extracts, suggested that acetonitrile and benzonitrile degradation may have occurred via nitrile hydratase and nitrilase pathways, respectively. Both the acetonitrile- and benzonitrile-degrading enzyme systems were significantly more thermostable in whole-cell preparations and cell-free extracts compared to their mesophilic counterparts.

show abstract

Section: Growth and Activity Profilesmentioning

confidence: 81%

Novel thermophilic bacteria producing nitrile-degrading enzymes

1997

View full text Add to dashboard Cite

show abstract

“…Riffel and Brandelli (2006) reported that keratinase producing bacteria had different characteristics, such as a broad temperature range of growth. The optimal proteolytic activities were detected between 30 and 37°C (Atalo and Gashe, 1993). An optimum keratin-degrading activity at mesophilic temperatures should be a desirable characteristic because these microorganisms may achieve hydrolysis with reduced energy input.…”

Section: Discussionmentioning

confidence: 93%

Biochemical and Molecular Characterization of a New Local Keratinase Producing Pseudomomanas sp., MS21

Tork¹,

Aly²,

Nawar³

2009

Asian J. of Biotechnology

View full text Add to dashboard Cite

This study aimed to isolate and identify a new local bacterial strain, able to completely degrade keratin-rich wastes into soluble and useful materials which can be used in many proposes. Bacterial keratinases are of particular interest because of their action on insoluble keratin substrates and generally on a broad range of protein substrates. These enzymes have been studied for de-hairing processes in the leather industry and hydrolysis of feather and keratin. Samples from poultry industry wastes, soil, water, fodder and feather were collected from different places in Jeddah, Saudi Arabia. Each sample was plated on feather meal agar plates containing 5 g LG feather as the sole carbon and nitrogen source and 1 the obtained colonies were selected, purified and their growth were detected on skimmed milk agar and feather meal broth media. The well grown isolates on feather meal agar which producing the largest clearing zone on skimmed milk plate were selected for keratinase assays. Out of 23 bacterial isolates, 7 isolates were selected. The best keratinase producing bacterium kera MS21 was selected and identified based on morphological, physiological and some biochemical characteristics. It was recorded as a species belonging to the genus Pseudomonas and identified as Pseudomonas sp. The results of identification were confirmed by 16S rDNA studies. Precipitation and purification of the keratinase enzyme in addition to factors affecting enzyme activity were studied. The enzyme molecular weight was determined to be of 30 KDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The optimum temperature and pH were determined to be 37°C and pH 8.0, respectively. The effect of some proteases inhibitors and activators were also studied.

show abstract

“…One organism may secrete variable amount and types of enzymes depending upon the pH and composition of medium (Kubackova et al, 1975) and most of the Bacillus species are known to grow in the fermentation medium having alkaline pH (Szumacher et al, 2004). Atalo et al (1993) has also reported that maximum protease enzyme production was obtained from Bacillus species at pH 9.5.…”

Section: Effect Of Different Diluentsmentioning

confidence: 89%

“…After that, the enzyme production starts to decrease which can be attributed to the decreased supply of nutrients to microorganisms (Romero et al, 1998). Bacillus species are known to produce maximum amount of proteases in the stationary phase or post exponential phase of their growth (Atalo and Gashe, 1993;Sharipova et al, 2000). However, some other Bacilli synthesize proteases during the exponential growth phase, but it mainly depends on the composition of the medium and some other factors.…”

Section: Effect Of Incubation Periodmentioning

confidence: 99%

Production of alkaline protease by Bacillus subtilis using solid state fermentation

Imtiaz¹,

Mukhtar²,

Ikram-ul-Haq³

2013

Afr. J. Microbiol. Res.

View full text Add to dashboard Cite

The present study describes the optimization of nutritional and cultural parameters for the production of alkaline protease by Bacillus subtilis under solid state conditions. Among cultural conditions, incubation temperature, incubation period and moisture level of the substrate were optimized and it was found that maximum production of alkaline protease was observed at 37°C and moisture to substrate ratio of 1:1 after 48 h of incubation period. Among different nutritional parameters, the effects of different diluents, carbon and nitrogen sources on the enzyme production were studied. Maximum enzyme production (101.23 U/g) was observed when D 2 {(% w/v) CaCO 3 , 0.05; peptone, 0.1; glucose, 0.1 and yeast extract, 0.1} was used to moisten the substrate. The best carbon source for the production of alkaline protease by B. subtilis was found to be sucrose at a concentration of 1%. Similarly, nutrient broth (1.5%) and diammonium hydrogen phosphate (0.1%) were found to be best organic and inorganic nitrogen sources, respectively. It was also found that the maximum protease (126.8 U/g) was produced when 25% (v/w) inoculum was used to inoculate the fermentation flasks.

show abstract

Protease production by a thermophilic Bacillus species (P-001A) which degrades various kinds of fibrous proteins

Cited by 79 publications

References 10 publications

Novel thermophilic bacteria producing nitrile-degrading enzymes

Novel thermophilic bacteria producing nitrile-degrading enzymes

Biochemical and Molecular Characterization of a New Local Keratinase Producing Pseudomomanas sp., MS21

Production of alkaline protease by Bacillus subtilis using solid state fermentation

Contact Info

Product

Resources

About