Skip to main content
Article thumbnail
Location of Repository

Optimization of Acid Protease Production by Aspergillus niger I1 on Shrimp Peptone Using Statistical Experimental Design

By Rayda Siala, Fakher Frikha, Samiha Mhamdi, Moncef Nasri and Alya Sellami Kamoun


Medium composition and culture conditions for the acid protease production by Aspergillus niger I1 were optimized by response surface methodology (RSM). A significant influence of temperature, KH2PO4, and initial pH on the protease production was evaluated by Plackett-Burman design (PBD). These factors were further optimized using Box-Behnken design and RSM. Under the proposed optimized conditions, the experimental protease production (183.13 U mL−1) closely matched the yield predicted by the statistical model (172.57 U mL−1) with R2 = 0.914. Compared with the initial M1 medium on which protease production was 43.13 U mL−1, a successful and significant improvement by 4.25 folds was achieved in the optimized medium containing (g/L): hulled grain of wheat (HGW) 5.0; KH2PO4 1.0; NaCl 0.3; MgSO4(7H2O) 0.5; CaCl2 (7H2O) 0.4; ZnSO4 0.1; Na2HPO4 1.6; shrimp peptone (SP) 1.0. The pH was adjusted at 5 and the temperature at 30°C. More interestingly, the optimization was accomplished using two cheap and local fermentation substrates, HGW and SP, which may result in a significant reduction in the cost of medium constituents

Topics: Research Article
Publisher: The Scientific World Journal
OAI identifier:
Provided by: PubMed Central
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://www.pubmedcentral.nih.g... (external link)
  • Suggested articles


    1. (1996). a r e l a ,M .D .F e r r a r i ,L .B e l o b r a j d i c ,R .W e y r a u c h ,a n d L. Loperena, “Short communication: effect of medium composition on the production by a new Bacillus subtilis isolate of protease with promising unhairing activity,”
    2. (2000). Advances in microbial amylases,”
    3. (2006). Amylase and protease production from A.
    4. (2003). An overview on fermentation, downstream processing and properties of microbial alkaline proteases,”
    5. An oxidantand solvent-stable protease produced by bacillus cereus SV1: application in the deproteinization of shrimp wastes and as a laundry detergent additive,”
    6. (2004). Application of statistical experimental design for optimization of alkaline protease production from Bacillus sp.
    7. (2010). Application of statistical experimental design for optimization of keratinases production by Bacillus pumilus A1 grown on chicken feather and some biochemical properties,”
    8. (1995). Aspartic proteinase from Penicillium camemberti: purification, properties, and substrate specificity,”
    9. Bacterial alkaline proteases: molecular approaches and industrial applications,” Applied MicrobiologyandBiotechnology,vol.59,no.1,pp.15–32,2002.
    10. (2009). Characterisation of acid protease expressed from
    11. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4,”
    12. (1992). Definition, characteristics and potential in solid state cultivation,”
    13. (1997). Disruption of three acid proteases in Aspergillus niger—effects on protease spectrum, intracellular proteolysis, and degradation of target proteins,”
    14. (2010). Enhanced Bacillus cereus BG1 protease production by the use of sardinelle (Sardinella aurita)p o w d e r ,
    15. (2009). Enhancement of sensitivity of molecularly imprinted polymer based parathion voltammetric sensor by using experimental design techniques,”
    16. (2009). Extracellular acid protease from Aspergillus niger I1: purification and characterization,”
    17. (2005). Extracellular acid protease from Rhizopus oryzae: purification and characterization,”
    18. (1993). F.L.Garcia-Carreno,L.E.Dimes,andN.F.Haard,“Substrategel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors,”
    19. (2000). Industrial media and fermentation processes for improved growth and protease production by Tetrahymena thermophila,”
    20. (1993). Kumagai,“Cloningandnucleotidesequenceoftheacidprotease-encoding gene (pepA) from Aspergillus oryzae,”
    21. (2002). L´ e c h e n n e ,C .Z a u g g ,M .H o l d o m
    22. (2001). Lysine aminopeptidase of Aspergillus niger,”
    23. (1999). Microbial alkaline proteases: from a bioindustrial viewpoint,”
    24. (1998). Molecular and biotechnological aspects of microbial proteases,”
    25. (2010). Nasri,andA.S.Kamoun,“Low-costfermentationmediumfor alkaline protease production by Bacillus mojavensis A21 using hulled grain of wheat and sardinella peptone,”
    26. (2002). O.Kirk,T.V.Borchert,andC.C.Fuglsang,“Industrialenzyme applications,” Current Opinion in Biotechnology,
    27. (2008). Optimisation of work roll grinding using Response Surface Methodology and evolutionary algorithm,”
    28. (2005). Optimization and scale up of production of alkaline protease from
    29. (2006). Optimization of a growth medium using a statistical approach for the production of an alkaline protease from a newly isolated Bacillus sp.
    30. (2004). Optimization of culture parameters for extracellular protease production from a newly isolated Pseudomonas sp. using response surface and artificialneuralnetworkmodels,”ProcessBiochemistry,vol.39,
    31. (2003). Optimization of medium and cultivation
    32. (1999). Optimization of milk-clotting enzyme productivitybyPenicilliumoxalicum,”
    33. (2008). OptimizationofalkalineproteaseproductionbyAspergillusclavatusES1 in Mirabilis jalapa tuber powder using statistical experimental design,”
    34. (2009). Optimized reuse and bioconversion from retentate of prefiltered palm oil mill effluent (POME) into microbial protease by Aspergillus terreus using response surface methodology,”
    35. (1980). Partial purification and characterization of a yeast extracellular acid protease,”
    36. (1997). Production of alkaline protease by an alkaliphilic bacteria isolated from an alkaline soda lake,”
    37. (2009). Production of alkaline protease from cellulosimicrobium cellulans,”
    38. (2001). Production of protease by Bacillus subtilis grown on sardinelle heads and viscera flour,”Bioresource Technology,
    39. (1988). Production of protease by Bacillus subtilis using simultaneous control of glucose and ammonium concentrations,”
    40. (1985). Profiles of alkaline protease production as a function of composition of the slant, age, transfer and isolate number and physiological state of culture,”
    41. (1998). Purification and characterization of acid proteinase from Neosartorya fischeri var.
    42. (1990). Purification and characterization of an extracellular acid proteinase from the ectomycorrhizal fungus Hebeloma crustuliniforme,”
    43. (1968). Purification and properties of Mucor pusillus acid protease,”
    44. (2003). Response surface methodological approach to optimize the nutritional parameters for neomycin production by
    45. (1993). Salt-tolerant and thermostable alkaline protease from Bacillus subtilis
    46. (2003). Some physicochemical properties of acid protease produced during growth of Aspergillus niger
    47. (1973). Some properties of acid protease from the thermophilic fungus,
    48. (1989). Statistical problem solving,” in Experimental Design in Biotechnology,P .D .H a a l a n d ,E d .
    49. (2001). Studies on production of thermostable alkaline protease from thermophilic and alkaliphilic Bacillus sp.
    50. (1946). The design of optimum multifactorial experiments,”
    51. (2010). The use of an economical medium for the production of alkaline serine proteases by Bacillus licheniformis NH1,”
    52. (1999). Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive,”
    53. (2000). UseofBox-Behnken designofexperimentsintheproduction of manganese peroxidase by Phanerochaete chrysosporium (MTCC 767) and decolorization of crystal violet,”

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.