Enzyme Microb. Francis, F. Gangadharan, D. Response surface methodology for the optimization of alpha amylase production by Bacillus amyloliquefaciens Bioresour Technol 99, Gavrilescu, M. Biotechnology-a sustainable alternative for chemical industry. Biotechnol Adv 23, Ghorai, S. Fungal biotechnology in food and feed processing. Food Res. Glymph, J. Production, purification, and characterization of alpha-amylase from Thermomonospora curvata.
Appl Environ Microbiol 34, Gomes, I. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus : production and partial characterization. Bioresour Technol 90, Goto, C.
Production of amylase by Aspergillus fumigatus utilizing alpha-methyl-D-glycoside, a synthetic analogue of maltose, as substrate. Goyal, N. I-3 and its use in the direct hydrolysis of raw potato starch. Gupta, R. Process Biochem 38, - Hamilton, L. IMD Process Biochem 35, Purification and properties of the raw starch degrading -amylase of Bacillus sp. Amylase production by Aspergillus niger in submerged cultivation on two wastes from food industries. Hmidet, N. Biochemical Engineering Journal 47, Hutcheon, G.
Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica Extremophiles 9, Ikram ul, H. Production of alpha amylase by Bacillus licheniformis using an economical medium. Bioresour Technol 87, Iulek, J.
Purification, biochemical characterisation and partial primary structure of a new alpha-amylase inhibitor from Secale cereale rye. Int J Biochem Cell Biol 32, Jaspreet Singha, J. Factors influencing the physico-chemical, morphological, thermal and rheological properties of some chemically modified starches for food applications-A review.
Food Hydrocolloids 21, Jensen, B. Enzyme production in continuous cultivation by the thermophilic fungus, Thermomyces lanuginosus Biotechnology Letters 24, Jin, B. Kajiwara, Y. Kammoun, R. Application of a statistical design to the optimization of parameters and culture medium for alpha-amylase production by Aspergillus oryzae CBS Bioresour Technol 99, Kandra, L.
Journal of Molecular Structure Theochem , Kathiresan, K. Khoo, S. Purification and characterization of alpha-amylase from Aspergillus flavus. Folia Microbiol Praha 39, Kirk, O. Industrial enzyme applications. Curr Opin Biotechnol 13, Konsoula, Z. Co-production of alpha-amylase and beta-galactosidase by Bacillus subtilis in complex organic substrates.
Bioresour Technol 98, Konsula, Z. Kunamneni, A. Amylase production in solid state fermentation by the thermophilic fungus Thermomyces lanuginosus J Biosci Bioeng , Mazzola, P. Liquid-liquid extraction of biomolecules: an overview and update of the main techniques.
J Chem Technol Biotechnol 83, Mitidieri, S. Enzymatic detergent formulation containing amylase from Aspergillus niger : a comparative study with commercial detergent formulations. Bioresour Technol 97, Mohapatra, B. Characterization of a fungal amylase from Mucor sp. Associated with the marine sponge Spirastrella sp. Moller, K. Production of fungal alpha-amylase by Saccharomyces kluyveri in glucose-limited cultivations. J Biotechnol , Moraes, L. Mukherjee, A. Murado, M.
Amylase production by solid state culture of Aspergillus oryzae on polyurethane foams. Some mechanistic approaches from an empirical model. Process Biochem 32, Muralikrishna, G. Carbohydrate Polymers 60, Nielsen, J. Protein engineering of bacterial alpha-amylases. Biochim Biophys Acta , Olsen, H. The Role of Enzymes in Modern Detergency. Journal of Surfactants and Detergents 1, Optimization of ethanol production from starch by an amylolytic nuclear petite Saccharomyces cerevisiae strain.
Yeast 23, Pandey, A. Advances in microbial amylases. Biotechnol Appl Biochem 31 Pt 2 , Payan, F. Structural basis for the inhibition of mammalian and insect alpha-amylases by plant protein inhibitors. Prakash, B. TVSP Process Biochem 44, Prakash, O. Appl Biochem Biotechnol ,. Human salivary amylase Which of the following is considered confirmatory for identifying saliva? Use of antihuman salivary amylase antiody b.
Phadebas assay c. RNA-based assay d. Starch-iodine assay Which of the following can distinguish human salivary amylase and human pancreatic amylase? RNA-based assay b. Use of antihuman salivary amylase antibody c. HCl: A. Homework Help 3,, Biology , Start filling in the gaps now. The genus Bacillus produces a large variety of extracellular enzymes, of which amylases are of particularly considerable industrial importance Swain et al.
Present study deals with the production condition optimization and partial characterization of crude extracellular amylase produced by Bacillus amyloliquefaciens P Zone of clearance due to the hydrolysis of starch. Screening of bacterial isolate for capability of amylase production was done by starch hydrolysis plate assay method. Therefore, further studies on enzyme production in shake-flask cultures were carried out using Bacillus amyloliquefaciens P The organism was used for extracellular amylase production in shake-flask culture using basal medium 0.
To enhance the production of enzyme various parameters associated with the production of amylase were studied in the medium used for the enzyme production. Among physical parameters, pH of the growth medium plays an important role in enzyme secretion. Most of the earlier studies revealed an optimum pH range between 6. Previous studies have revealed that fungi required slightly acidic pH and bacteria required neutral pH for optimum growth Gangadharan et al.
So, the effect of initial pH on the production of amylase by Bacillus amyloliquefaciens P was investigated at different pH 6. The activity of the enzyme was obtained at slightly alkaline pH 9. But, the final pH of the medium initial pH 9. It might be due to the fact that the enzyme was inactive in the acidic medium Castro et al. Another study conducted by O. El- Tayeb showed that alpha amylase production by Bacillus amyloliquefaciens strain CH in fermentor was highest at pH 6.
El-Tayeb et al. Effect of culture conditions for extracellular amylase production from Bacillus amyloliquefaciens P - in shake - flask cultivations. Bacterial amylases are produced at a much wider range of temperature. Bacillus amyloliquefaciens , B. Haq et al. The total protein content obtained was 3. A prolonged incubation time beyond 48 hour did not increase the enzyme production.
These findings are similar to the result reported by Haq et al. A similar result was also found by Asgher et al. DLB 9 and Riaz et al. It might be due to the accumulation of other by products in the medium Riaz et al.
Efficient induction might not occur until the stationary phase has been reached and the available carbon source was reduced Huang et al. But, Abate et al. Similar findings have been reported on Bacillus amyloliquefaciens Hillier et al.
ANT-6 Burhan et al. The volume of inoculum plays an important role in the fermentation of enzymes Lin et al. As the inoculum level was further increased, the production of enzyme was gradually decreased. It may be due to the fact that at high concentration of inoculum level, the bacteria grow rapidly and the nutrients present in the media were insufficient to overcome the growth of bacteria.
Thus, the production of amylase was affected at higher concentration of inoculum. Our findings are in a good agreement with Riaz et al. Natural sources could serve as economical and readily available raw material for the production of valuable enzymes. Agricultural wastes are being used for liquid fermentation to reduce the cost of fermentation media. These wastes consist of different carbon sources are necessary for the growth of microorganisms Haq et al.
The nature and amount of carbon sources in culture media are important factor for the production of extracellular amylase Akcan Biosynthesis of the enzyme took place not only in the presence of starch but also with other carbon sources.
Besides, rice flour and wheat bran showed moderate effects on enzyme synthesis. Earlier studies reported that, complex substrates induce higher amylase production Sexana et al. Effect of carbon sources on amylase production by Bacillus amyloliquefaciens P - Absorbance was measured at nm with spectrophotometer and Enzyme activity was presented on the y axis and carbon sources was on x axis.
The nature and relative concentration of different complex nitrogenous sources in the growth medium are both important in the synthesis of amylase. Lower levels of nitrogen and also excess nitrogen are equally detrimental causing enzyme inhibition Sharma et al. The influence of organic nitrogen sources on amylase production was determined. Among the different organic nitrogen sources tested, tryptone 0.
In fact, tryptone has been reported to be the best nitrogen source for amylase production Okalo et al. In present study, yeast extract, casein and beef extract also showed stimulating effects on amylase synthesis. It was observed that inorganic nitrogen sources gave comparatively higher yields than organic nitrogen sources. In present study, the enzyme production was increased when ammonium nitrate used as inorganic nitrogen source in the culture media. It has also been reported that, ammonium nitrate and sodium nitrate were the best nitrogen sources for maximum amylase production Kundu et al.
Ammonium chloride, ammonium sulphate showed stimulating effects on amylase production. Swain et al. Effect of organic nitrogen source on amylase production by Bacillus amyloliquefaciens P - Different organic nitrogen sources 0. Enzyme activity was presented on the y axis and organic nitrogen sources was on x axis. Effect of inorganic nitrogen source on amylase production by Bacillus amyloliquefaciens P - To determine the effect of inorganic nitrogen sources on enzyme production different inorganic nitrogen sources were used 0.
A pH range from 5. In the alkaline pH range, the activity was lower. For determination of optimum reaction time, enzyme assay was carried out at different reaction time ranging from 5—50 minutes at constant temperature and pH.
Aygan et al. Stability of the enzyme is of great importance for the economy of their industrial application. In case of thermostabilty, the enzyme was pre incubated at different temperatures for 30 min and then enzyme was assayed.
Thus, the results concluded that the crude enzyme is moderately temperature stable. It is therefore worthwhile to consider means to stabilize the enzyme under storage conditions. Temperature is an important limiting factor for storage of enzymes. In our study, enzyme was stored at room temperature for 21 days. But, the room temperature was moderately suitable for the storage of this enzyme in considering commercialization and industrial application, thus causing the rapid reduction of enzyme activity.
Effect of pH on enzyme activity. For determination of optimum assay pH of the enzyme reaction, 0. The enzyme activity was measured and the results are presented on graph. Effect of temperature on enzyme activity. To study the effect of temperature on enzyme reaction activity, the enzyme reaction was carried out at different temperatures for 10 min in a shaking water bath and results are presented on graph.
Effect of reaction time on enzyme activity. To investigate the optimum reaction period of the enzyme solution, reaction was carried out using 0. The results are presented on graph.
Thermal stability of enzyme. For the determination of thermostability of amylase, 1 ml of sodium phosphate buffer pH 6.
0コメント