نتایج جستجو برای: thermostable enzyme

تعداد نتایج: 243447  

Journal: :Biodiversitas 2022

Abstract. Fazal BZ, Budiman C, Amin Z, Ling CMW. 2022. Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia. Biodiversitas 23: 2807-2815. Thermostable ?-amylases are being used in a wide range industries, including food, textiles, detergents, pharmaceuticals, fine chemicals. A good source thermostable thermophilic is found high-temperat...

2017
Nawel Boucherba Mohammed Gagaoua Amel Bouanane-Darenfed Cilia Bouiche Khelifa Bouacem Mohamed Yacine Kerbous Yacine Maafa Said Benallaoua

The present study investigates the production and partial biochemical characterization of an extracellular thermostable xylanase from the Bacillus oceanisediminis strain SJ3 newly recovered from Algerian soil using three phase partitioning (TPP). The maximum xylanase activity recorded after 2 days of incubation at 37 °C was 20.24 U/ml in the presence of oat spelt xylan. The results indicated th...

Journal: :Archives of biochemistry and biophysics 1961
A S SUSSMAN

The differences between a thermostable (T”) and thermolabile ( TL) form of tyrosmase from Neurospora crassa have been studied by means of a spectrophotometric technique using ascorbate or ferrocyanide. No significant differences in substrate specificit> have been found in a survey of over 30 substances which included mono-, di-, tri-, and conjugated phenols. Catechol was found to be a substrate...

2010
Meenakshi Gursharan Singh Aditya Bhalla Gurinder Singh Hoondal

Bacillus sp. MG-33 was isolated from the desert of Rajasthan (India). The organism produced 500 and 200 Ug of thermostable mannanase (after 96h) in solid state fermentation (SSF) of wheat bran and wheat straw rich-soda pulp at the moisture ratio of 1:1.5 and 1:3 at 30oC, respectively. Two-step partially purified mannanase was optimally active at 65oC and was 100% thermostable at 55 to 60oC for ...

2014
Aleardo Morelli John Haugner Burckhard Seelig

Artificial enzymes hold the potential to catalyze valuable reactions not observed in nature. One approach to build artificial enzymes introduces mutations into an existing protein scaffold to enable a new catalytic activity. This process commonly results in a simultaneous reduction of protein stability as an undesired side effect. While protein stability can be increased through techniques like...

2003
S. LORING

Since the discovery by Jones (1) of a thermostable enzyme in the pancreas, capable of hydrolyzing ribonucleic acid without the release of either phosphoric acid or purine bases, the evidence as to the nature of its action has been extremely conflicting. Jones and Perkins isolated four mononucleotides from enzyme-treated nucleic acid and concluded that the action of the enzyme consisted in break...

Journal: :The Journal of biological chemistry 2003
Takashi Hatta Gouri Mukerjee-Dhar Jiri Damborsky Hohzoh Kiyohara Kazuhide Kimbara

A novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl-1,2-dioxygenase (BphC_JF8) catalyzing the meta-cleavage of the hydroxylated biphenyl ring was purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8, and the gene was cloned. The native and recombinant BphC enzyme was purified to homogeneity. The enzyme has a molecular mass of 125 +/- 10 kDa and was composed...

Journal: :Molecular pharmacology 2009
Daquan Gao Diwahar L Narasimhan Joanne Macdonald Remy Brim Mei-Chuan Ko Donald W Landry James H Woods Roger K Sunahara Chang-Guo Zhan

Enhancing cocaine metabolism by administration of cocaine esterase (CocE) has been recognized as a promising treatment strategy for cocaine overdose and addiction, because CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine yet identified. A major obstacle to the clinical application of CocE is the thermoinstability of native CocE with a half-life of only a...

Journal: :Applied and environmental microbiology 2013
Xi Wu Chong Zhang Izumi Orita Tadayuki Imanaka Toshiaki Fukui Xin-Hui Xing

A novel thermostable alcohol dehydrogenase (ADH) showing activity toward aromatic secondary alcohols was identified from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (TkADH). The gene, tk0845, which encodes an aldo-keto reductase, was heterologously expressed in Escherichia coli. The enzyme was found to be a monomer with a molecular mass of 31 kDa. It was highly thermostable wi...

Journal: :Antioxidants 2023

An ultrasound-enzyme-assisted extraction (UEAE) was optimized to extract, simultaneously, the hydrophilic and lipophilic compounds from three berry pomaces (raspberry, strawberry blackberry). First, an enzyme screening designated a thermostable alkaline protease as most suitable recover, in aqueous medium, highest yields of polyphenols oil efficient way. Secondly, selected coupled ultrasounds (...

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