A highly thermostable alkaline amylase producing Bacillus sp. PN5 was isolated from soil, which yielded 65.23 U mL(-1) of amylase in medium containing (%) 0.6 starch, 0.5 peptone and 0.3 yeast extract at 60 degrees C, pH 7.0 after 60 h of incubation. Maximum amylase activity was at pH 10.0 and 90 degrees C. The enzyme retained 80% activity after 1 h at pH 10.0. It exhibited 65% activity at 105 degrees C and had 100% stability in the temperature range between 80 and 100 degrees C for 1 h. In addition, there was 86.36% stability after 1-h incubation with sodium dodecylsulphate. These properties indicated possible use of this amylase in starch saccharification and detergent formulation.
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http://dx.doi.org/10.1016/j.biortech.2006.01.016 | DOI Listing |
JACS Au
December 2024
School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Wangchan Valley, Rayong 21210, Thailand.
Biocatalysis has emerged as a green approach for efficient and sustainable production in various industries. In recent decades, numerous advancements in computational and predictive approaches, including ancestral sequence reconstruction (ASR) have sparked a new wave for protein engineers to improve and expand biocatalyst capabilities. ASR is an evolution-based strategy that uses phylogenetic relationships among homologous extant sequences to probabilistically infer the most likely ancestral sequences.
View Article and Find Full Text PDFJ Appl Glycosci (1999)
November 2024
1 Matsutani Chemical Industry Co., Ltd.
D-Allulose 3-epimerase catalyzes C-3 epimerization between D-fructose and D-allulose was found in strain M30. The enzyme gene was cloned, and its recombinant enzyme and the mutant variants were expressed in Using the information of the sequence and model structure, we succeed in the improvement of melting temperature for the enzyme without significant loss of the enzyme activity by protein engineering method. The melting temperatures were increased by 2.
View Article and Find Full Text PDFEnzyme Microb Technol
December 2024
Department of Biotechnology, Lorena School of Engineering, University of São Paulo, Lorena, SP, Brazil. Electronic address:
β-glucosidases (BGLs) are key enzymes in the depolymerization of cellulosic biomass, catalyzing the conversion of cello-oligosaccharides into glucose. This conversion is pivotal for enhancing the production of second-generation ethanol or other value-added products in biorefineries. However, the process is often cost-prohibitive due to the high enzyme loadings required.
View Article and Find Full Text PDFArch Biochem Biophys
December 2024
Department of Biology and Biotechnology, University of Pavia, Via Ferrata 9, 27100, Pavia, Italy. Electronic address:
Bacterial monoamine oxidases (MAOs) are FAD-dependent proteins catalyzing a relevant reaction for many industrial biocatalytic applications, ranging from production of enantiomerically pure building blocks for pharmaceutical synthesis to biosensors for monitoring food and beverage quality. The thermostable MAO enzyme from Thermoanaerobacterales bacterium (MAO) is about 36 % identical to both putrescine oxidase and human MAOs and can be efficiently produced in Escherichia coli. MAO preferentially acts on n-alkyl monoamines but shows detectable activity also on polyamines and aromatic monoamines.
View Article and Find Full Text PDFBioorg Chem
December 2024
Northeast Asia Academy, Changchun University of Chinese Medicine, Changchun 130117, PR China. Electronic address:
A novel GH1 β-glucosidase Fpglu1 from Fervidobacterium pennivorans DSM9078 was successfully cloned and expressed in Escherichia coli. This hyperthermophilic enzyme possesses unique features that make it valuable in biochemistry and pharmacology. It exhibited optimal activity at temperatures exceeding 100 °C, a trait rarely observed in other enzymes, and demonstrated extraordinary thermostability.
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