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Amylase (Production and application0
- 1. Seminar on Amylase- Productionand Application Arun Kumar Gupta Department of Food Engineering and Technology
- 2. Introduction Amylases (E.C. 3.2.1.1.)are starch- degrading enzymes that catalyze the hydrolysis glycosidic bonds in polysaccharides.
- 3. Year Inventor Amylase/other 1811Kirchoff Amylase 1833 Anselme Payen Diastases 1894 - Fungal source 1917 Biodin and Effront B. subtilis & B. mesenteroids 1930 Ohlsson β-amylase 1952 Kuhn Named α-amylase 1990 - 3-D Crystal Structure
- 4. Types of amylase Theseenzymes are classified as per their action on the glycosidic bond. • α-amylase (E.C. 3.2.1.1) • β-amylase (E.C. 3.2.1.2) • γ-amylase (E.C. 3.2.1.3) • α-Glucosidase (E.C. 3.2.1.20)
- 5. 1. Endoamylases: Cleaveinternal α-1,4 bonds resulting in α anomeric products. 2. Exoamylases: Cleave α-1,4 or a-1,6 bonds of the external glucose residues resulting in α or β anomeric products. 3. Debranching enzymes: Hydrolyse α-1,6 bonds exclusively leaving long linear polysaccharides. 4. Transferases: Cleave α-1,4 glycosidic bond of the donor molecule and transfer part of the donor to a glycosidic acceptor forming a new glycosidic bond. Function of Amylase
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- 7. Source of Production Plant •Not considered a significant source for the commercial production of amylase. • Agricultural wastes are used in the production. Animal • Ptyalin, a salivary α-amylase (40% total salivary protein ) • Calcium containing metalloenzyme, hydrolyzes α-1,4 linkages of starch. Microbial • Fungal (Aspergillus niger, Aspergillus oryzae, Penicillium, Thermomyces lanuginosus) • Bacterial (Bacillus spp.)
- 8. Fermentative production Used toconvert moist agricultural polymeric into fermented food products. It is simple technique, low capital investment, lower levels of catabolite repression and end-product inhibition, low waste water output, better product recovery, and high quality production. In this, enzymes and other reactive compounds are submerged in a liquid such as alcohol, oil or a nutrient broth. The process is used for a variety of purposes, mostly in industrial manufacturing.
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- 10. Outline of enzymeproduction from microorganism Source:https://www.google.co.in/search?rlz=1C1NHXL_enIN767IN767&biw=1366&bih=623&tbm=isch&sa=1&ei=S60BWr2MAsfP0gSryLTQDA&q=fermentation+proces s+of+amylase&oq=fermentation+process+of+amy&gs_l=psy-ab.3.0.0i24k1.973549.987151.0.988311.29.28.1.0.0.0.417.4754.0j11j9j1j1.22.0....0...1.1.64.psy- ab..6.23.4818...0j0i67k1j0i13k1j0i30k1.0.yQ9dARk6UhE#imgrc=q_crK4bYkfyW-M:
- 11. Unitoperation Upstream Fermentation Downstream Inoculum Sterilization of Fermenter Inoculation MediaSterilization Media Transfer Controlled Growth Level Monitoring Prevention of contamination Protection Termination Separation, Isolation and Purification Effluent Treatment
- 12. Physical & ChemicalFactor • Temperature • Period of incubation • Carbon sources acting • Nitrogen sources • Phosphate • Moisture and • Agitation • pH • Surfactants • Minerals and metal ion • Inducers
- 13. Temperature • Growth ofthe organism • Amylase production at optimum at 50–55 °C for the thermophilic fungal cultures such as Talaromyces emersonii, Thermomonospora fusca and Thermomyces lanuginosus. • At 37–60 °C, Mesophilic fungal culture such as Bacillus amyloliquefaciens, B. subtilis, B. licheniformis and B. stearothermophilus. • Rhodothermus marinus, a marine thermophilic bacterium.
- 14. Stoichiometry equation Placket BurmannDesign To find the independent variable which produce large effect. Carbon Source + Energy Requirement + Oxygen + Nitrogen + Other Requirement Biomass + Product+ Water + Heat + Carbon Dioxide =
- 15. Carbon Sources Carbon sourcessuch as galactose, glycogen and inulin suitable for B. licheniformis and Bacillus sp. maltose, a- methyl -D-glucoside, resulted in 3-fold higher a- amylase production.
- 16. Nitrogen media • Soyabean meal - Bacillus sp. Strains of B. stearothermophilus and B. amylolyticus secreted maximum a-amylase in a medium supplemented with 1 % peptone, 0.5 % yeast extract and 0.5 % maltose under vigorous shaking conditions. • Yeast extract also resulted in significant a-amylase yield. • Addition of corn steep liquor and ammonium hydrogen phosphate to SSF involving Amaranthus grains as substrate by A. flavus gave high enzyme yield.
- 17. Moisture • Most importantparameters in SSF that influences the growth of the organism and thereby enzyme production. • a-Amylase production by Bacillus licheniformis was highest with 65 % initial moisture content in an SSF system. • High Moisture content = Decrease production
- 18. pH • It determinesthe growth and morphology of microorganisms as they are sensitive to the concentration of hydrogen ions present in the medium. • pH is known to affect the synthesis and secretion of a-amylase just like its stability. • pH=5.0–6.0 = A. oryzae, A. ficuum and A. niger = significant yields • pH=5.0 = Saccharomyces cerevisiae and S. kluyveri = maximum enzyme production. • pH=7.0 = Clostridium thermosulfurogenes = maximum yield
- 19. Surfactants Increase the secretionof proteins by increasing cell membrane permeability. Increase the production of extracellular enzymes. Ex: Tween 20, SDS
- 20. Down stream Processing Centrifugation Disk bowl centrifuge Tubular Filtration Simple Leaffilter Plate and Frame Cell disruption Physical Liquid shear Solid shear Freezing & thawing Ultra sonication Chemical Osmotic shock Alkali treatment Detergent Biological Enzyme Cell Separation Floatation Flocculation Chromatography Drying
- 21. Purification Downstream processing forthe production of pure enzymes can generally constitute a major percentage of overall production cost. Purification processes in downstream processing after fermentation strongly depend on the market, processing cost, final quality, and available technology.
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- 23. Production of Glucose and Maltosesyrup *DE is a measure of the amount of reducing sugars present in a sugar product, relative to dextrose (glucose).
- 25. References Tiwari, S. P.,Srivastava, R., Singh, C. S., Shukla, K., Singh, R. K., Singh, P., Singh, R., Singh, N. L. and Sharma, R. (2015). Amylase: An Overview with special references to alpha amylase. Journal of Global Biosciences, Vol. 4, Spl. Issue 1.