scholarly journals Investigation on a Bangladeshi isolate Bacillus aryabhattai for promising biotechnological applications

2018 ◽  
Vol 7 (2) ◽  
pp. 33-45
Author(s):  
Mohammad Shahedur Rahman ◽  
Rasheda Banu ◽  
Ripa Moni ◽  
Nazmul Islam ◽  
Mastura Khatun Ruma ◽  
...  
Keyword(s):  
Soil Sample ◽  
Extracellular Enzymes ◽  
Extreme Conditions ◽  
Biotechnological Applications ◽  
Optimum Temperature ◽  
First Report ◽  
Bacillus Aryabhattai ◽  
Physico Chemical ◽  
Chemical Studies

A new isolate was investigated from soil sample collected from Shahrasti upazilla of Chandpur district of Bangladesh. Based on the physico-chemical studies the strain was identified as gram positive Bacilli. Moleculer characterization of the strain was identified as Bacillus aryabhattai which is the first report in Bangladesh. The strain can survive in extreme conditions of salt, temperature and pH. This strain was further characterized and screened for the ability to produce useful enzymes. The optimum temperature for growth and production of these enzymes was within the temperature range 35oC to 40oC. The pH was found to be 7 for its growth and production of different enzymes when investigated over 48 h of incubation. The isolate produced various extracellular enzymes such as α-amylases, cellulases, β-glucosidases, lipases and proteases. The findings of this study provide useful information of the new strain that has potential biotechnological applications. Jahangirnagar University J. Biol. Sci. 7(2): 33-45, 2018 (December)

scholarly journals BIOCHEMICAL CHARACTERIZATION OF RECOMBINANT PHYTASE ENZYME (phyK) FROM Klebsiella sp. ASR1 ENCAPSULATED WITH ALGINATE

2020 ◽  
Vol 7 (1) ◽  
Author(s):  
Muhammad Eka Hidayatullah ◽  
. Sajidan ◽  
Ari Susilowati ◽  
Baraka Stewart Mkumbe ◽  
Ralf Greiner
Keyword(s):  
Metal Ion ◽  
Biochemical Characterization ◽  
Extreme Conditions ◽  
Optimum Temperature ◽  
High Ph ◽  
Recombinant Phytase ◽  
Ion Effects ◽  
Metal Ion Effects

Karakterisasi Biokimia Enzim Fitase Rekombinan (phyK) dari Klebsiella sp. ASR1 Yang Dienkapsulasi Dengan AlginatEnzim fitase melepas molekul fosfor pada atom C dari benzena Inositol fitat. Tetapi fitase memiliki kelemahan tidak mampu bertahan terhadap kondisi ekstrim dalam lambung nonruminansia. Solusi dalam penelitian ini yaitu fitase dienkapsulasi menggunakan alginat. Penelitian ini bertujuan mengkarakterisasi fitase setelah dienkapsulasi menggunakan alginate. Hasil penelitian ini yaitu fitase yang dienkapsulasi memiliki aktivitas tertinggi pada pH 6,0, sedangkan fitase tanpa enkapsulasi pada pH 5,0. Suhu optimum untuk aktivitas tertinggi fitase yang dienkapsulasi yaitu 70ºC, sedangkan fitase tanpa enkapsulasi 37ºC. Untuk perlakuan penambahan ion logam, aktivitas tertinggi fitase yang dienkapsulasi terjadi dengan penambahan 0,1 mM Fe2+ dan 1,0 mM Ca2+, sedangkan fitase tanpa enkapsulasi dengan penambahan 0,1 mM Fe2+. Berdasarkan hasil penelitian ini, fitase yang dienkapsulasi memiliki keunggulan lebih banyak dibandingkan dengan fitase tanpa enkapsulasi, karena mampu bertahan pada pH dan suhu tinggi, dan beberapa efek ion logam.Kata Kunci: alginat, asam fitat, enkapsulasi, fitase, fitase rekombinanABSTRACTPhytase enzymes release phosphorus molecules on the C atom from benzene inositol phytate. But phytase has the disadvantage of being unable to withstand extreme conditions in the non-ruminant stomach. The solution in this research was phytase encapsulated using alginate. This study aims to characterize phytase after being encapsulated using alginate. The results of this study were the encapsulated phytase had the highest activity at pH 6.0, while the unencapsulated phytase at pH 5.0. The optimum temperature for the highest activity of the encapsulated phytase was 70ºC, while the unencapsulated phytase 37ºC. For treatment of metal ion addition, the highest activity of the encapsulated phytase occurred with the addition of 0.1 mM Fe2+ and 1.0 mM Ca2+, while the unencapsulated phytase with the addition of 0.1 mM Fe2+. Based on the results of this study, the encapsulated phytase had more advantages compared to the unencapsulated phytase, as the former withstand high pH and temperature, and some metal ion effects.

scholarly journals Synthesis and Structural Characterization of Lanthanum(III) Complexes of 4-Nitrosoantipyrine

2021 ◽  
Vol 33 (3) ◽  
pp. 617-621
Author(s):  
Meera Gopal ◽  
Sreesha Sasi
Keyword(s):  
Magnetic Susceptibility ◽  
Spectral Data ◽  
General Formula ◽  
Structural Characterization ◽  
Bidentate Ligand ◽  
Bidentate Ligands ◽  
Nitroso Group ◽  
Physico Chemical ◽  
Chemical Studies

A new series of La(III) complexes of the ligand with the general formula [La(L)2(a)3] and [La2(L)4(aa)3], (a = nitrate (1), thiocyanate (2), acetate (3) and propionate (4) ions, aa = sulphate (5), thiosulphate (6), oxalate (7) and malonate (8) ions with the ligand 4-nitrosoantipyrine (L) were synthesized and characterized using various physico-chemical studies. The primary ligand L acts as a bidentate ligand utilizing the carbonyl group and the nitroso group for bonding. The nitrate, thiocyanate, acetate and propionate ions are monovalent unidentate ligands, whereas sulphate, thiosulphate, oxalate and malonate ions are divalent bidentate ligands in the complexes 1-8. Based on spectral data and magnetic susceptibility measurements, geometry of the lanthanum(III) complexes were also proposed.

scholarly journals Purification and characterization of a novel thermostable β-amylase from Clostridium thermosulphurogenes

1988 ◽  
Vol 254 (3) ◽  
pp. 835-840 ◽  
Author(s):  
G J Shen ◽  
B C Saha ◽  
Y E Lee ◽  
L Bhatnagar ◽  
J G Zeikus
Keyword(s):  
Catalytic Properties ◽  
Amylase Activity ◽  
Soluble Starch ◽  
Single Type ◽  
Optimum Temperature ◽  
Purification And Characterization ◽  
Enzyme Thermostability ◽  
Physico Chemical ◽  
Hydrophobic Amino Acids

An extracellular beta-amylase from Clostridium thermosulphurogenes was purified 811-fold to homogeneity, and its general molecular, physico-chemical and catalytic properties were determined. The native enzyme was a tetramer of 210 kDa composed of a single type subunit; its 20 amino acid N-terminus displayed 45% homology with Bacillus polymyxa beta-amylase. The beta-amylase was enriched in both acidic and hydrophobic amino acids. The pure enzyme displayed an isoelectric point of 5.1 and a pH activity optimum of 5.5. The optimum temperature for beta-amylase activity was 75 degrees C, and enzyme thermostability at 80 degrees C was enhanced by substrate and Ca2+ addition. The beta-amylase hydrolysed amylose to maltose and amylopectin and glycogen to maltose and limit dextrins, and it was inhibited by alpha- and beta-cyclodextrins. The enzyme displayed kcat. and Km values for boiled soluble starch of 400,000 min-1 per mol and 1.68 mg/ml, respectively. The enzyme was antigenically distinct from plant beta-amylases.

scholarly journals Physico-chemical Studies on Iodine-Complexes of Amilase and Starch-Fractions for Characterization of Polysaccharides

1969 ◽  
Vol 72 (2) ◽  
pp. 526-531
Author(s):  
Takashi HANDA ◽  
Hideo AIKAWA ◽  
Tadahiro ISHII ◽  
Reikichi ORIGASA ◽  
Yaichi AYUKAWA
Keyword(s):  
Physico Chemical ◽  
Chemical Studies ◽  
Iodine Complexes

scholarly journals Characterization of Humic Acid and Fulvic Acid Extracted from Soil Samples of Cultivated Areas of North Bengal and Sikkim States, India

2020 ◽  
Vol 33 (1) ◽  
pp. 62-66
Author(s):  
M. Chanda ◽  
S. Jha ◽  
D. Mukhopadhyay ◽  
M. Pandey
Keyword(s):  
Humic Acid ◽  
Organic Carbon ◽  
Fulvic Acid ◽  
Chemical Properties ◽  
Available Phosphorus ◽  
Physico Chemical ◽  
Chemical Studies ◽  
Measurement Surface ◽  
North Bengal

Humic acid and fulvic acid extracted from soils of cultivated areas, collected from Majitar, Darjeeling and Pundibari cities were first isolated, purified and then characterized for the physico-chemical properties (oxidizable organic carbon, electrical conductivity, pH, phosphorus, nitrogen, potassium, CEC, etc.). The physico-chemical studies showed that soils were neutral to acidic but are independent of altitude. Organic carbon, available phosphorus, nitrogen were higher with soil of Majitar city. The total acidity, carboxylic group, phenolic -OH group were higher in fulvic acid than in humic acid. Further, both acids were characterized by potentiometric titration, viscometric measurement, surface tension and spectral analysis. The humification index (E4/E6) of fulvic acid was relatively higher than humic acid. The highest molecular weight of humic acid and fulvic acid were recorded 13645.83 and 1465.54, respectively.

scholarly journals Characterization of EstDR4, a Novel Cold-Adapted Insecticides-Metabolizing Esterase from Deinococcus radiodurans

2021 ◽  
Vol 11 (4) ◽  
pp. 1864
Author(s):  
Yage Zhang ◽  
Wei Lu ◽  
Jin Wang ◽  
Ming Chen ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Deinococcus Radiodurans ◽  
Tween 80 ◽  
Pharmaceutical Products ◽  
High Catalytic Activity ◽  
Biotechnological Applications ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Cold Adapted ◽  
Triton X

Cold-adapted esterases are attracting increasing attention owing to their prospective use in biotechnology. In this study, a novel cold-adapted family Ⅳ esterase EstDR4 was identified and obtained from extremophile Deinococcus radiodurans (D. radiodurans). EstDR4 displayed significant substrate preference towards short and medium chain monoesters (C2–C12). It also showed regioselectivity, enantioselectivity and degradation effects on four insecticides. The optimum temperature and pH for EstDR4 activity were 30 °C and pH 8, respectively. Additionally, EstDR4 exhibited relatively high catalytic activity at 0 °C and high stability from 10–40 °C, with over 80% of its initial activity retained after 1 h of incubation. Moreover, EstDR4 activity was stimulated by Tween 80 and Triton X-100, and inhibited by metal ions such as Co2+, Cu2+ and Zn2+ and several organic solvents. Thus, this enzyme shows development potential for many industrial biotechnological applications, including the manufacture of thermolabile pharmaceutical products, cold-wash detergents and insecticide biodegradation.

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