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Lichenase (
EC3.2.1.73, licheninase, β-(1→4)-D-glucan 4-glucanohydrolase, 1,3, 1,4-β-glucan endohydrolase, 1,3, 1,4-β-glucan 4-glucanohydrolase, 1,3-1,4-β-D-glucan 4-glucanohydrolase) is an
enzyme with
systematic name(1→3)-(1→4)-β-D-glucan 4-glucanohydrolase.[1][2] It was named after its activity in on
lichenin (a form of mixed-linkage glucan).
The best-characterised variant of this of enzyme is Bacillus subtilis lichenase, which is used as a molecular biology tool in determining the structure of mixed-linkage glucans.[3][4][5][6] This variant cleaves (1,4) bonds that immediately follow a (1,3) bond.[7]
Other lichenases have different specificities, for example Aspergillus japonicus lichenase cleaves (1,4) bonds that immediately precede a (1,3) bond.[8]
^Barras DR, Moore AE, Stone BA (1969). "Enzyme-Substrate Relationships Among β-Glucan Hydrolases". Cellulases and Their Applications. Advances in Chemistry. Vol. 95. pp. 105–138.
doi:
10.1021/ba-1969-0095.ch008.
ISBN0-8412-0095-5.
^McCleary, Barry V; Codd, Rachel (1991). "Measurement of (1 → 3),(1 → 4)-β-D-glucan in barley and oats: A streamlined enzymic procedure". Journal of the Science of Food and Agriculture. 55 (2): 303–312.
Bibcode:
1991JSFA...55..303M.
doi:
10.1002/jsfa.2740550215.
ISSN0022-5142.
^Mangan, D.; Liadova, A.; Ivory, R.; McCleary, B. V. (2016-11-29). "Novel approaches to the automated assay of β-glucanase and lichenase activity". Carbohydrate Research. 435: 162–172.
doi:
10.1016/j.carres.2016.10.006.
ISSN0008-6215.
PMID27810709.
^Yoo, Dong-Hyung; Lee, Byung-Hoo; Chang, Pahn-Shick; Lee, Hyeon Gyu; Yoo, Sang-Ho (2007-03-01). "Improved Quantitative Analysis of Oligosaccharides from Lichenase-Hydrolyzed Water-Soluble Barley β-Glucans by High-Performance Anion-Exchange Chromatography". Journal of Agricultural and Food Chemistry. 55 (5): 1656–1662.
doi:
10.1021/jf062603l.
ISSN0021-8561.
PMID17284049.
^Hrmova, Maria; Fincher, Geoffrey B. (2009-01-01), Bacic, Antony; Fincher, Geoffrey B.; Stone, Bruce A. (eds.), "Chapter 3.1 - Plant and Microbial Enzymes Involved in the Depolymerization of (1,3)-β-D-Glucans and Related Polysaccharides", Chemistry, Biochemistry, and Biology of 1-3 Beta Glucans and Related Polysaccharides, Academic Press, pp. 119–170,
doi:
10.1016/B978-0-12-373971-1.00004-2,
ISBN9780123739711
^McCleary, Barry V. (1988-01-01). "Lichenase from Bacillus subtilis". Biomass Part A: Cellulose and Hemicellulose. Methods in Enzymology. Vol. 160. Academic Press. pp. 572–575.
doi:
10.1016/0076-6879(88)60170-4.
ISBN9780121820619.
^Grishutin, Sergei G.; Gusakov, Alexander V.; Dzedzyulya, Ekaterina I.; Sinitsyn, Arkady P. (2006). "A lichenase-like family 12 endo-(1→4)-β-glucanase from Aspergillus japonicus: study of the substrate specificity and mode of action on β-glucans in comparison with other glycoside hydrolases". Carbohydrate Research. 341 (2): 218–229.
doi:
10.1016/j.carres.2005.11.011.
PMID16343463.
This article needs additional or more specific
categories. Please
help out by
adding categories to it so that it can be listed with similar articles.(April 2024)
This article needs attention from an expert in Biology or Molecular Biology. The specific problem is: Article is too confusing for the average reader.WikiProject Biology or
WikiProject Molecular Biology may be able to help recruit an expert.(April 2024)
Lichenase (
EC3.2.1.73, licheninase, β-(1→4)-D-glucan 4-glucanohydrolase, 1,3, 1,4-β-glucan endohydrolase, 1,3, 1,4-β-glucan 4-glucanohydrolase, 1,3-1,4-β-D-glucan 4-glucanohydrolase) is an
enzyme with
systematic name(1→3)-(1→4)-β-D-glucan 4-glucanohydrolase.[1][2] It was named after its activity in on
lichenin (a form of mixed-linkage glucan).
The best-characterised variant of this of enzyme is Bacillus subtilis lichenase, which is used as a molecular biology tool in determining the structure of mixed-linkage glucans.[3][4][5][6] This variant cleaves (1,4) bonds that immediately follow a (1,3) bond.[7]
Other lichenases have different specificities, for example Aspergillus japonicus lichenase cleaves (1,4) bonds that immediately precede a (1,3) bond.[8]
^Barras DR, Moore AE, Stone BA (1969). "Enzyme-Substrate Relationships Among β-Glucan Hydrolases". Cellulases and Their Applications. Advances in Chemistry. Vol. 95. pp. 105–138.
doi:
10.1021/ba-1969-0095.ch008.
ISBN0-8412-0095-5.
^McCleary, Barry V; Codd, Rachel (1991). "Measurement of (1 → 3),(1 → 4)-β-D-glucan in barley and oats: A streamlined enzymic procedure". Journal of the Science of Food and Agriculture. 55 (2): 303–312.
Bibcode:
1991JSFA...55..303M.
doi:
10.1002/jsfa.2740550215.
ISSN0022-5142.
^Mangan, D.; Liadova, A.; Ivory, R.; McCleary, B. V. (2016-11-29). "Novel approaches to the automated assay of β-glucanase and lichenase activity". Carbohydrate Research. 435: 162–172.
doi:
10.1016/j.carres.2016.10.006.
ISSN0008-6215.
PMID27810709.
^Yoo, Dong-Hyung; Lee, Byung-Hoo; Chang, Pahn-Shick; Lee, Hyeon Gyu; Yoo, Sang-Ho (2007-03-01). "Improved Quantitative Analysis of Oligosaccharides from Lichenase-Hydrolyzed Water-Soluble Barley β-Glucans by High-Performance Anion-Exchange Chromatography". Journal of Agricultural and Food Chemistry. 55 (5): 1656–1662.
doi:
10.1021/jf062603l.
ISSN0021-8561.
PMID17284049.
^Hrmova, Maria; Fincher, Geoffrey B. (2009-01-01), Bacic, Antony; Fincher, Geoffrey B.; Stone, Bruce A. (eds.), "Chapter 3.1 - Plant and Microbial Enzymes Involved in the Depolymerization of (1,3)-β-D-Glucans and Related Polysaccharides", Chemistry, Biochemistry, and Biology of 1-3 Beta Glucans and Related Polysaccharides, Academic Press, pp. 119–170,
doi:
10.1016/B978-0-12-373971-1.00004-2,
ISBN9780123739711
^McCleary, Barry V. (1988-01-01). "Lichenase from Bacillus subtilis". Biomass Part A: Cellulose and Hemicellulose. Methods in Enzymology. Vol. 160. Academic Press. pp. 572–575.
doi:
10.1016/0076-6879(88)60170-4.
ISBN9780121820619.
^Grishutin, Sergei G.; Gusakov, Alexander V.; Dzedzyulya, Ekaterina I.; Sinitsyn, Arkady P. (2006). "A lichenase-like family 12 endo-(1→4)-β-glucanase from Aspergillus japonicus: study of the substrate specificity and mode of action on β-glucans in comparison with other glycoside hydrolases". Carbohydrate Research. 341 (2): 218–229.
doi:
10.1016/j.carres.2005.11.011.
PMID16343463.
This article needs additional or more specific
categories. Please
help out by
adding categories to it so that it can be listed with similar articles.(April 2024)