Articles

Kinetics of alkaline protease production by Streptomyces griseoflavus PTCC1130

Abstract

Background and Objectives: Proteases are a group of enzymes that catalyze the degradation of proteins resulting in the pro- duction of their amino acid constituents. They are the most important group of industrial enzymes which account for about 60% of total enzymes in the market and produced mainly by microorganisms. The attempts were made to study the kinetic parameters of protease produced by Streptomyces griseoflavus PTCC1130.
Materials and Methods: Streptomyces griseoflavus PTCC1130 was grown on casein agar. Different media such as BM1, BM2, BM3 and BM4 were prepared. Data obtained from growth and protease production were subjected to kinetics evalu- ation. Casein was used as substrate for protease activity and the released soluble peptide bearing aromatic amino acid were quantified by Folin Cioclateaue reagent. Protein content of the enzyme and the sugar utilized by the organism were estimated by Bradford and Miller’s methods respectively.
Results: Basal Medium named as BM1, BM2, BM3 and BM4(50 mL in 250 mL Erlen Meyer flasks) were screened out to evaluate protease production by Streptomyces griseoflavus PTCC1130. They were inoculated with known amount of seed culture and kept on rotary shaker. To obtain the specific growth rate, wet weight of biomass was plotted against the time. The clarified supernatant was used for the analysis of protease by measuring the soluble peptide containing aromatic amino acid residues employing Folin Cioclateaue reagent. Our results showed that maximum level of enzyme production (14035 U/L) was occurred at late exponential phase using Basal Medium supplemented with zinc sulfate (0.5g/L), casein (10g/L) at pH 6.5.
Conclusions: A kinetic study of protease production by Streptomyces griseoflavus PTCC1130 provided highly quantitative information regarding the behavior of a system, which is essential to study the fermentation process. Exploitation of such kinetics analysis would be useful in commercialization of microbial enzyme production.

Mohamed Abdel-Aziz S, Ahmed Hamed A, Mohamed Ghaly F, Hanaa El-Shafei A. Purification and charac- terization of alkaline protease from marine Streptomy- ces albidoflavus. J Appl Sci Res 2012; 8 :3707-3716.

Jayasree D, Sandhya Kumara TD, Kavi Kishor PB, Vi- jaya Lakshmi M, Lakshmi Narasu M. Optimization of production protocol of alkaline protease by Streptomy- ces pulvereceus. Inter JRI Sci Technol 2009; 1: 79- 82.

Debananda Ningthoujam S, PintubalaShetri K, Sana- sam S , Nimaichand S. Screening, identification of best producers and optimization of extracellular proteases from moderately halophilic alkali thermo tolerant in- digenous Actinomycetes. World Appl Sci J 2009; 7:907-916.

Singhal P, NigamVK, VidyarthiAS. Studies on produc- tion, characterization and applications of microbial al- kaline proteases. Int J Adv Biotecnol Res 2012; 3: 653-669.

Mukesh Kumar DJ, Premavathi V, Govindarajan N, Balakumaran MD, Kalaichelvan PT. Production and purification of alkaline protease from Bacillus sp. MPTK 712 isolated from dairy sludge. Global Veter- inaria 2012; 8: 433-439.

El-Shafei HanaA, Abdel-Aziz Mohamed S, Ghaly Mohamed F, Abdalla Ahmed AH. Optimizing some factors affecting alkaline protease production by a ma- rine bacterium Streptomyces albidoflavus. Proceed- ing of fifth environmental conference ZAGAZIG UNI 2010;125-142.

Mohapatre BR, Bapuji M, Sree A. Production of indus- trial enzymes (amylase, carboxy methyl cellulase and protease) by bacteria isolated from marine sedentary organisms. Acta Biotechnol 2003; 23:75-84.

Bhunia B, Bikram B, Pinaki B, Apurba D. Kinetic studies of alkaline protease from Bacillus licheniform- is NCIM-2042. J Microbiol Biotechnol 2012; 22:1758–1766.

Rajendran A,Thangavelu V. Evaluation of unstructured kinetic models for the production of protease by Bacil- lus sphaericus MTCC11. Eng Life Sci 2008; 8: 179-175.

Krishnaveni K, Mukesh Kumar DJ, Balakumaran MD, RameshS, Kalaichelvan PT. Production and optimiza- tion of extracellular alkaline protease from Bacillus subtilis isolated from dairy effluent. Der Pharmacia Letter 2012;4:98-109.

Narayana K J P ,Vijayalakshmi M. Production of extra- cellular protease by Streptomyces albidoflavus. Asian J Biochem 2008; 3:198-202.

Mehta VJ, Thamar JT, Singh SP. Production of alkaline protease from an alkaliphilic actinomycetes. Biore- source Technology 2006;97: 1650-1654.

Mitra P,Chakrabartty P K. An extracellular protease with depilation activity from Streptomyces nogalator.J Sci Ind Res 2005; 64: 978-983.

Gupta R, Beg QK, Khan S, Chauhan B. An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl Microbiol Biotech- nol 2002;60:381–395.

Miller GL. Use of dinitrosalicylic acid reagent for deter- mination of reducing sugar. Anal Chem 1959;31:426–428.

Whiteley CG, Lee DJ. Enzyme technology and bio- logical remediation. Enzyme Microb Technol 2006;38:291–316.

Ikram-ul-Haq, Mukhtar H. Biosynthesis of prote- ase from Lactobacillus paracasei: Kinetic analysis of fermentation parameters. Ind J Biochem Biophys 2006;43:377-381.

Gaden Jr, Elmer L. Fermentation process kinetics. Bio- technol Bioeng 2000;67: 629-635.

Wahid S, Ferdous J, Anwar MN. Factors influencing the production and properties of extracellular protease from Streptomyces bikiniensis. The Chittagong Univ J B Sci 2009;4(1&2): 153-163.

Mostafa Sayed E, Saad Moatazam E, Awad Hassan M, Selim Mohsen H, Helmy H. Optimization conditions of extracellular proteases production from a newly iso- lated Streptomyces Pseudogrisiolus NRC-15. E-Jour- nal of Chemistry 2012; 9:949-961.

Files
IssueVol 8 No 1 (2016) QRcode
SectionArticles
Keywords
microbial enzyme kinetics of fermentation Streptomyces griseoflavus

Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
How to Cite
1.
Hosseini SV, Saffari Z, Farhanghi A, Atyabi SM, Norouzian D. Kinetics of alkaline protease production by Streptomyces griseoflavus PTCC1130. Iran J Microbiol. 2016;8(1):8-13.