Statistical optimization of medium components for extracellular protease production by an extreme haloarchaeon,<i>Halobacterium</i>sp. SP1(1)

Akolkar, Aparna V.; Bharambe, Nikhil; Trivedi, Shruti; Desai, Anjana J.

doi:10.1111/j.1472-765x.2008.02492.x

Cited by 24 publications

(15 citation statements)

References 18 publications

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“…3 Time course of growth, protease production and change in pH by Streptomyces sp. A6 in 5-l bench fermenter reported by Akolkar et al (2009) in which interaction between protein source (soybean flour) and FeCl 3 was highly significant. The fact that the interaction effect between pH and ZnSO 4 was also significant indicated their importance in protease production by Streptomyces sp.…”

Section: Discussionmentioning

confidence: 93%

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Optimization of protease production by Streptomyces sp. A6 using statistical approach for reclamation of shellfish waste

Singh

Chhatpar

2010

World J Microbiol Biotechnol

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Protease producing Streptomyces sp. A6 was isolated from intertidal zone of the coast of Diu (Gujarat, India). Plackett-Burman method was applied to identify important factors (shrimp waste, FeCl 3 , ZnSO 4 and pH) influencing protease production by Streptomyces sp. A6. Further optimization was done by response surface methodology using central composite design. The concentrations of medium components for higher protease production as optimized using the above approach were (g l -1 ): Shrimp waste, 14; FeCl 3 , 0.035; ZnSO 4 , 0.065 and pH, 8.0. This statistical optimization approach led to production of 129.02 ± 2.03 U ml -1 of protease which was 4.96 fold higher compared to that obtained using the unoptimized medium. The protease production was scaled to 3 l in a 5-l bench fermenter using optimized medium which further increased the production by 63.4%. Deproteinization and chitin recovery obtained at the end of fermentation was 85.12 ± 4.7 and 70.58 ± 1.33%, respectively. The present study is the first report on statistical optimization of medium components for production of protease by Streptomyces species using cheaper raw material such as shrimp waste. The study also explored the possibility Streptomyces sp. A6 for reclamation of shrimp wastes.

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Section: Discussionmentioning

confidence: 93%

“…No previous reports are available on effect of ZnSO 4 on protease production by Streptomyces species. Akolkar et al (2009) has reported 1.54 fold increase in protease production by Halobacterium sp. SP1(1) in presence of FeCl 3 .…”

Section: Discussionmentioning

confidence: 98%

Optimization of protease production by Streptomyces sp. A6 using statistical approach for reclamation of shellfish waste

Singh

Chhatpar

2010

World J Microbiol Biotechnol

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“…A similar result was reported in Halobacterium sp. SP1(1) (Akolkar et al 2009). The protease activity was relatively stable in the temperature range of 60-65°C and retained 85.2% of its activity at 70°C (El-Hawary and Ibrahim, 1992).…”

Section: Discussionmentioning

confidence: 98%

“…including, Halobacterium halobium (Izotova et al 1983), Halobacterium sp. SP(1) (Akolkar et al 2009), Halobacterium sp. Js1 (VijayAnand et al 2010), and many strains of Halobacterium salinarum isolated from habitats like Thai fish sauce, salted fish and hides, solar salterns, estuaries polluted with crude oil etc (Thongthai and Suntinanalert 1991).…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis optimization and purification of a solvent stable alkaline serine protease from Halobacterium sp.

Vijayaraghavan

Jebamalar²,

Vincent

2011

Ann Microbiol

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Three halotolerant bacterial isolates that were isolated from the salt pan of coastal Tamilnadu, India, were screened on skimmed milk agar plates containing 1-25% (w/v) NaCl for protease secretion. Among the three positive isolates, Halobacterium sp. showed the maximum protease secretion (4.5 mm diameter zone) and was hence selected for this study. The enzyme was a serine protease as evidenced by complete inactivation of enzyme after treatment with a serine protease inhibitor (phenylmethylsulfonyl fluoride). Culture conditions which optimize protease production that included pH, fermentation period, NaCl in addition to different factors such as carbon and nitrogen sources, casein concentration were investigated. Optimum bacterial growth and proteolytic activity was achieved after 48 h of incubation at 37°C, pH 10.0 with 5% (w/v) NaCl concentration and 2.5% (w/v) casein. Initial experiments revealed that the culture medium containing 1.0% (w/v) lactose as the carbon source and 1.0% (w/v) ammonium chloride as the nitrogen source supported maximized enzyme production. Analysis carried out using SDS-PAGE revealed that the extracellular enzyme consisted of a single polypeptide chain of 43 kDa which was purified by a combination of ammonium sulphate fractionation, DEAE cellulose and Sephadex G-75 gel filtration chromatography. This protease was stable for a wide range of temperatures (40-60°C), NaCl concentrations (1-5%, w/v) and pH (8.0-10.0) with maximal activity observed at 60°C, 5% NaCl and pH 10.0. Proteolytic activity was enhanced by 1.0 mM of Ca 2+ (137%) and strongly inhibited by Mn 2+ (67%). Most importantly, the proteolytic activity remained stable in alkaline pH and was found to be active at higher temperatures. The broad range of temperature optima with respect to enzyme activity was indicative of this enzymes suitability in fish sauce fermentation, which was carried out at 35-45°C. This enzyme was stable in organic solvents such as toluene and hexane and the relative enzyme activity was 103 and 114%, respectively, which mainly finds use in the paint industry.

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“…Numerous studies on optimum media composition (Akolkar et al, 2009;Singh et al, 2009;Ghorbel-Bellaaj et al, 2012) have been investigated but no such research has been reported with Lysobacter capsici YS1215 on the production of chitinase and gelatinase in a systematic way. Therefore, the present investigation was carried out to optimize the medium composition for chitinase and gelatinase production using RSM.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Medium Components for the Production of Antagonistic Lytic Enzymes Against Phytopathogenic Fungi and Their Biocontrol Potential

Lee¹,

Neung²,

Park³

et al. 2014

Korean Journal of Soil Science and Fertilizer

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In this paper, fractional factorial screening design (FFSD) and central composition design (CCD) were used to optimize the medium components for producing chitinase and gelatinase by Lysobacter capsici YS1215. Crab shell powder, nutrient broth and gelatin were proved to have significant effects on chitinase and gelatinase activity by FFSD first. An optimal medium was obtained by using a three factor CCD, which consisted of nutrient broth of 2.0 g L ). This value was 3.76 and 1.11 fold of the chitinase and gelatinase activity, respectively, compared to the lowest productive medium in the design matrix. In investigating potential of these enzymes partially purified from L. capsici YS1215 for biotechnological use, the crude enzymes was found to be inhibition against pathogenic fungal mycelia: Colletotrichum gleosporioides, Phytophthora capsici, and Rhizoctonia solani. In this study, we demonstrated the optimal medium for producing the chitinolytic and gelatinolytic enzymes by the strain YS1215 and the role of their enzymes that may be useful for further development of a biotechnological use and agricultural use for biological control of phytopathogenic fungi.

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Statistical optimization of medium components for extracellular protease production by an extreme haloarchaeon,Halobacteriumsp. SP1(1)

Cited by 24 publications

References 18 publications

Optimization of protease production by Streptomyces sp. A6 using statistical approach for reclamation of shellfish waste

Optimization of protease production by Streptomyces sp. A6 using statistical approach for reclamation of shellfish waste

Biosynthesis optimization and purification of a solvent stable alkaline serine protease from Halobacterium sp.

Optimization of Medium Components for the Production of Antagonistic Lytic Enzymes Against Phytopathogenic Fungi and Their Biocontrol Potential

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