Enzymatic synthesis of banana flavour (isoamyl acetate) by Bacillus licheniformis S-86 esterase

Torres, Sebastián; Baigorí, Mario Domingo; Swathy, Sasidharan L.; Pandey, Ashok; Castro, Guillermo R.

doi:10.1016/j.foodres.2008.12.005

Cited by 88 publications

(55 citation statements)

References 48 publications

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“…Similar results were also reported for esterases of Streptococcus thermophiles and Bacillus licheniformis S-86 [28,33]. respectively [34].…”

Section: Effect Of Some Metal Ions On the Enzyme Activitysupporting

confidence: 85%

Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Akatin

2015

Turk J Bioch

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Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425 T [Thermus sp. NCCB 100425 T ' den yeni bir ısıya dayanıklı esterazın saflaştırılması ve karakterizasyonu] ABSTRACT Objective: The purpose of the present study was to purify and characterize an esterase from a thermophilic bacterium Thermus sp. NCCB 100425 T and to check its suitability for industrial applications. Methods: Thermus sp. NCCB 100425 T esterase was purified by using ammonium sulphate precipitation and hydrophobic interaction chromatography and then characterized biochemically. Results: The purity of the enzyme was observed as a single band on native-and SDS-PAGE. In the presence of p-nitrophenyl acetate (pNPA) as a substrate, the optimum pH and temperature of the enzyme were found to be 7.5 and 60°C, respectively. K m and V max values are calculated as 18.32 mM and 96.15 U/mg protein, respectively, with pNPA. pH stability was investigated in the range of pH 4.0-9.0 at 4°C and 60°C. After 7 days incubation, activity of pure enzyme was retained 85-90% for all pH at 4°C and 59±5.2% for pH 8.0 at 60°C. It was determined that approximately 80% of enzyme activity was retained between 30-60°C after 7 days incubation. In the presence of 10% ethanol and DMSO, the enzyme activity was retained 96±2.7% and 78±2.5%, respectively. Additionally, it was detected that some metal ions affect the enzyme activity at different ratios. T esterazı amonyum sülfat çöktürmesi ve hidrofobik etkileşim kromatografisi kullanılarak saflaştırıldı ve biyokimyasal özellikleri incelendi. Bulgular: Doğal-ve SDS-PAGE'de tek bant şeklinde görülen saf enzimin, p-nitrofenil asetat (pNPA) varlığında optimum pH ve sıcaklık değerleri sırasıyla 7,5 ve 60°C olarak belirlendi. Yine pNPA bir substrat olarak kullanıldığında K m ve V max değerlerinin 18,32 mM ve 96,15 U/ mg protein olduğu tespit edildi. pH kararlılığı pH 4,0-9,0 aralığında 4°C ve 60°C'de incelendi. 7 günlük bir inkübasyondan sonra saf enzimin aktivitesinin 4°C'de bütün pH'larda yaklaşık %85-90 oranında korunduğu, bu oranın 60°C'de pH 8,0'de ise %59±5,2 olduğu görüldü. 30-60°C'ler arasında 7 gün inkübe edilen enzim, orijinal aktivitesini %80 oranında korudu. %10 nihai konsantrasyondaki etanol ve DMSO varlığında enzim aktivitesi sırasıyla %96±2,7 ve %78±2,5 oranlarında korundu. Ayrıca, bazı metal iyonlarının enzim aktivitesini farklı oranlarda etkilediği tespit edildi. Sonuç: Bütün bu sonuçlar değerlendirildiğinde Thermus sp. NCCB 100425 T esterazının özel-likle yüksek sıcaklık-ve pH-kararlılığı nedeniyle endüstriyel ve/veya klinik uygulamalar için avantajlara sahip olabileceği açıkça görülmektedir. Thus, this study can be considered as a step to obtain an industrially suitable esterase having excellent features. ) and solvents were purchased from Merck A.G. (Darmstadt, Germany). All chemicals were analytical and microbiological grade. Conclusion Materials and Methods Chemicals Bacterial strain and crude enzyme extractionThermus sp. NCCB 100425 T bacterial strain isolated from a geotherm...

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“…Similar results were also reported for esterases of Streptococcus thermophiles and Bacillus licheniformis S-86 [28,33]. respectively [34].…”

Section: Effect Of Some Metal Ions On the Enzyme Activitysupporting

confidence: 85%

Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Akatin

2015

Turk J Bioch

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“…The thermal stability of esterase from Geobacillus sp. TF17 was found higher than that observed in esterases from B. licheniformis S-86 (50% at 50°C for 1 h) [31] and Bacillus sp. (50% at 65°C for 10 h) [22], nearly similar with P. furiosus (100% 75°C for 2 h) [34] but lower than Thermus thermophilus HB27 esterase (50% at 85°C for 135 min) [35].…”

Section: Ph-and Thermal-stabilitymentioning

confidence: 57%

“…However, the optimum temperature of Geobacillus sp TF17 esterase is higher than the esterases from Cucurbita pepo Elc and Ell with an optimum temperature between 30 and 40°C [30] and some Bacillus sp. with an optimum temperature at 45°C [17], and is lower than the esterase from Bacillus licheniformis S-86 [31] at 60°C and Fervidobacterium nodosum Rt17-B1 [32] at 75°C.…”

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 83%

Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Çolak

2013

Turk J Bioch

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“…Ethyl valerate (green apple flavour), ethyl butyrate (pineapple favour) and isoamyl acetate (banana flavour) are synthesised through esterification of lipase enzyme [23]. The immobilized lipase enzyme was used for the above study and it was mainly obtained from Candida rugosa and porcine pancreas [24][25][26].…”

Section: Enzymes For the Synthesis Food Flavoursmentioning

confidence: 99%

Biosynthesis of Food Flavours and Fragrances - A Review

Poornima¹,

Preetha²

2017

Asian J. Chem.

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Enzymatic synthesis of banana flavour (isoamyl acetate) by Bacillus licheniformis S-86 esterase

Cited by 88 publications

References 48 publications

Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Purification and characterization of a novel thermostable esterase from Thermus sp. NCCB 100425T

Purification and characterization of a pH and heat stable esterase from Geobacillus sp. TF17

Biosynthesis of Food Flavours and Fragrances - A Review

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