A new member of family 8 polysaccharide lyase chondroitin AC lyase (PsPL8A) from Pedobacter saltans displays endo- and exo-lytic catalysis

Aruna Rani, A. Goyal
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引用次数: 12
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来自盐田土杆菌(Pedobacter saltans)的8家族多糖裂解酶软骨素AC裂解酶(PsPL8A)的新成员具有内溶和外溶的催化作用
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来源期刊
Journal of Molecular Catalysis B-enzymatic
Journal of Molecular Catalysis B-enzymatic 生物-生化与分子生物学
CiteScore
2.58
自引率
0.00%
发文量
0
审稿时长
3.4 months
期刊介绍: Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation. Papers should report novel and significant advances in one or more of the following topics; Applied and fundamental studies of enzymes used for biocatalysis; Industrial applications of enzymatic processes, e.g. in fine chemical synthesis; Chemo-, regio- and enantioselective transformations; Screening for biocatalysts; Integration of biocatalytic and chemical steps in organic syntheses; Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies; Enzyme immobilization and stabilization, particularly in non-conventional media; Bioprocess engineering aspects, e.g. membrane bioreactors; Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification; Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity; Biomimetic studies related to enzymatic transformations.
期刊最新文献
A highly efficient immobilized MAS1 lipase for the glycerolysis reaction of n-3 PUFA-rich ethyl esters A more polar N-terminal helix releases MBP-tagged Thermus thermophilus proline dehydrogenase from tetramer-polymer self-association Investigation of structural stability and enzymatic activity of glucose oxidase and its subunits A new member of family 8 polysaccharide lyase chondroitin AC lyase (PsPL8A) from Pedobacter saltans displays endo- and exo-lytic catalysis Special issue OxiZymes 2016
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