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Mohd Shukuri Mohamad Ali

Researcher at Universiti Putra Malaysia

Publications -  102
Citations -  1222

Mohd Shukuri Mohamad Ali is an academic researcher from Universiti Putra Malaysia. The author has contributed to research in topics: Lipase & Chemistry. The author has an hindex of 16, co-authored 82 publications receiving 746 citations. Previous affiliations of Mohd Shukuri Mohamad Ali include Forest Research Institute Malaysia.

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Adaptational properties and applications of cold-active lipases from psychrophilic bacteria.

TL;DR: Cold-evolved lipases from bacteria and their peculiar properties, in addition to their potential biotechnological and industrial applications, are discussed.
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Current Development in Decolorization of Synthetic Dyes by Immobilized Laccases.

TL;DR: The significance of laccase immobilization is highlighted and some of the challenges and opportunities of this technology are pointed out as a revolutionary biocatalytic solution to this environmental problem.
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The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

TL;DR: Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities, which provides a higher pH value and thermal stability for enzymes toward synthesis and facilitates enzymes used in a continuous process.
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The biology and the importance of Photobacterium species.

TL;DR: Photobacterium species are Gram-negative coccobacilli which are distributed in marine habitats worldwide and are considered a special group of bacteria because some species are capable of producing essential polyunsaturated fatty acids, antibacterial compounds, lipases, esterases and asparaginases.
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Isolation, Characterisation, and Lipase Production of a Cold-Adapted Bacterial Strain Pseudomonas sp. LSK25 Isolated from Signy Island, Antarctica.

TL;DR: This study focuses on bacterial strains isolated from anthropogenically-influenced soil samples collected around Signy Island Research Station, and found the highest level of sequence similarity to a Pseudomonas sp.