A Bacillus acidocaldarius .ALPHA.-amylase that is highly stable to heat under acidic conditions.

Kanno, Mutsuo

doi:10.1271/bbb1961.50.23

Cited by 27 publications

(14 citation statements)

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“…KR-8104 (Sajedi et al 2005), Bacillus sp. WN11 (Mamo and Gessesse 1999) and B. acidocaldarius (Kanno 1986). The pH adjustment step in the liquefaction and saccharification stages can be avoided by using Ca 2?…”

Section: Resultsmentioning

confidence: 99%

High maltose-forming, Ca2+-independent and acid stable α-amylase from a novel acidophilic bacterium, Bacillus acidicola

Sharma

Satyanarayana

2010

Biotechnol Lett

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Section: Resultsmentioning

confidence: 99%

High maltose-forming, Ca2+-independent and acid stable α-amylase from a novel acidophilic bacterium, Bacillus acidicola

Sharma

Satyanarayana

2010

Biotechnol Lett

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“…Nilai K m α-amilase TII-12 lebih kecil dibandingkan dengan α-amilase B. acidocaldarius A2 yang memiliki Km 1,6 mg/ml (Kanno, 1986). Hal ini menunjukkan bahwa α-amilase TII-12 untuk mencapai kecepatan maksimum memerlukan konsentrasi substrat lebih tinggi daripada α-amilase B. licheniformis BLM 1777.…”

Section: Sifat Kinetik Dan Bobot Molekul Enzimunclassified

Purifikasi dan Karakterisasi α-amilase Termostabil dari Bacillus stearothermophilus TII-12

et al. 2011

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Purification and Characterization of Thermostable α-amylase from Bacillus stearothermophilus TII-12. Puji Lestari, Nur Richana, Abdul A. Darwis, Khaswar Syamsu, and Untung Murdiyatmo. Thermostable α-amylase is a potential enzyme employed in the starch processing and widely used in food industries, but this enzyme is still imported. The local enzyme production would be more economist and useful for its broad applications. Here we report α-amylase from indigenous bacteria TII-12 which was purified and characterized, as well as analyzed its hydrolysis product on cassava starch. The enzyme of Bacillus stearothermophilus TII-12 partially purified by ultrafiltration, acetone precipitation and gel filtration (Sephadex G-100) showed the reduced total activity, total protein and yield, but increased the specific activity. The enzyme had a K m of 1,06 mg/ml and V max of 1,21 mol/min, with optimal activity at pH 7 and 90 o C. An apparent molecular mass was of 192.932,8 Dalton, as estimated by Native-Polyacrylamide Agarose Gel electrophoresis. Its activity was inhibited by the divalent cation chelator such as EDTA and CuSO 4 but activated by calcium ion. Hydrolysis products of this enzyme on cassava starch were glucose, dextrin, maltose and oligosaccharides. After 24 hours of hydrolysis, the concentration of glucose and maltose reached 51.970 and 10.090 ppm, respectively. The thermostable α-amylase of TII-12 is an endo-α-amylase and prospective to be applied on starch liquefaction with high temperature process.Keywords: Bacillus stearothermophilus, characterization, purification, thermostable α-amylase. ABSTRAK Purifikasi dan Karakterisasi α-amilase Termostabil dariBacillus stearothermophilus TII-12. Puji Lestari, Nur Richana, Abdul A. Darwis, Khaswar Syamsu, dan Untung Murdiyatmo. α-amilase termostabil merupakan enzim potensial yang banyak digunakan dalam pengolahan pati dan industri makanan, namun demikian enzim ini masih diimpor. Produksi enzim lokal akan menjadikan lebih ekonomis dan bermanfaat untuk aplikasinya secara lebih luas. Hak Cipta © 2011, BB-BiogenStudi ini melaporkan pemurnian, karakterisasi, dan analisis produk hidrolisis α-amilase dari bakteri TII-12 pada pati ubi kayu. Enzim dari Bacillus stearothermophilus TII-12 yang dimurnikan secara parsial dengan ultrafiltrasi, pengendapan aseton, dan gel filtrasi (Sephadex G-100) menunjukkan penurunan aktivitas total, protein total, dan rendemen, tetapi aktivitas spesifik meningkat. Enzim ini mempunyai K m sebesar 1,06 mg ml dan V max adalah 1,21 mol/menit, dengan aktivitas optimal pada pH 7,0 dan 90 o C. Berdasarkan estimasi menggunakan native-polyacrylamide agarose gel electrophoresis, masa molekul α-amilase dari bakteri TII-12 sekitar 192.932,8 Dalton. Aktivitas enzim ini dihambat oleh kelat kation divalen seperti EDTA dan CuSO4, tetapi meningkat aktivitasnya oleh ion kalsium. Produk hidrolisis enzim ini pada pati ubi kayu meliputi glukosa, dekstrin, maltosa, dan oligosakarida. Setelah 24 jam hidrolisis konsentrasi glukosa dan maltosa mencapai 51.970 dan 1...

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“…The genus Bacillus is considered an ideal host for the industrial production of bulk extracellular amylase. Several Bacillus species are involved in amylase production, such as Bacillus stearothermophilus (Kyoko et al 1970), Bacillus polymyxa (Sohn et al 1996), Bacillus licheniformis (Kanno 1986;Takasaki et al 1994), Bacillus subtilis (Riaz et al 2003) and Bacillus amyloliquefaciens (Khajeh et al 2006). Optimal culture conditions for amylase productivity have been studied by many investigators (Sivaramakrishnan et al 2006;Santos and Martins 2003;Saxena et al 2007).…”

Section: Introductionmentioning

confidence: 99%

“…Acid amylase from high yielding strains has been studied extensively (Kanno 1986;Zhang et al 1994;Wang et al 2008). One of the major drawbacks affecting the stability at acidic pH of enzymes recovered from thermophiles is that enzymes from thermophiles are stable over a wide pH range but are usually thermolabile.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of a novel, highly acid- and thermo-stable amylase from thermophilic Bacillus strain HUTBS62 under different environmental conditions

2011

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A novel, highly acid-and thermo-stable amylase was detected from culture medium of thermophilic Bacillus strain HUTBS62 isolated from a hot spring located near the Dead Sea, Jordan. The enzyme was purified by precipitation with 60% ammonium sulfate, gel filtration on Sephadex G-100 and DEAE ion exchange chromatography. The enzyme was purified 22.7-fold with 11.6% yield. Purified enzyme was a monomer with a molecular mass of 54.2 kDa. The optimum pH and temperature for catalytic activity was pH 4.4 and 90°C, respectively. Roughly 50% of amylase activity remained even after heat treatment for 90 min at 100°C; moreover 90% of the activity was retained after heat treatment for 2 h at 60°C. The half-life of the enzyme at 70°C, 80°C and 90°C was estimated to be 5, 4 and 2 h, respectively. The activation energy of denaturation of the purified enzyme was 3.29 kJ mol −1 . The presence of 5 mM metal ion affected amylase activity variably; for example: the presence of cobalt, magnesium, cadmium, and manganese increased amylase activity. On the other hand, iron and sodium decreased residual activity to different extents, while calcium, zinc and copper inhibited amylase activity. The enzyme was active in the presence of 1 and 2 mM EDTA at pH 4.4 and 90°C. The purified amylase was acid-and thermo-stable with novel properties making it suitable for many industrial food purposes.

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A Bacillus acidocaldarius .ALPHA.-amylase that is highly stable to heat under acidic conditions.

Cited by 27 publications

References 0 publications

High maltose-forming, Ca2+-independent and acid stable α-amylase from a novel acidophilic bacterium, Bacillus acidicola

High maltose-forming, Ca2+-independent and acid stable α-amylase from a novel acidophilic bacterium, Bacillus acidicola

Purifikasi dan Karakterisasi α-amilase Termostabil dari Bacillus stearothermophilus TII-12

Characteristics of a novel, highly acid- and thermo-stable amylase from thermophilic Bacillus strain HUTBS62 under different environmental conditions

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