Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa

Craig B. Faulds; Marie Christine Ralet; Gary Williamson; Geoffrey P. Hazlewood; Harry J. Gilbert

doi:10.1016/0304-4165(94)00140-S

Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa

Craig B. Faulds, Marie Christine Ralet, Gary Williamson, Geoffrey P. Hazlewood, Harry J. Gilbert

Research output: Contribution to journal › Article › Research › peer-review

37 Citations (Scopus)

Abstract

Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.

Original language	English
Pages (from-to)	265-269
Number of pages	5
Journal	BBA - General Subjects
Volume	1243
Issue number	2
DOIs	https://doi.org/10.1016/0304-4165(94)00140-S
Publication status	Published - 23 Feb 1995
Externally published	Yes

Keywords

(Pesudomonas)
Esterase
Ferulic acid
Oligosaccharide

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10.1016/0304-4165(94)00140-S

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title = "Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa",

abstract = "Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.",

keywords = "(Pesudomonas), Esterase, Ferulic acid, Oligosaccharide",

author = "Faulds, {Craig B.} and Ralet, {Marie Christine} and Gary Williamson and Hazlewood, {Geoffrey P.} and Gilbert, {Harry J.}",

year = "1995",

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language = "English",

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pages = "265--269",

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T1 - Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa

AU - Faulds, Craig B.

AU - Ralet, Marie Christine

AU - Williamson, Gary

AU - Hazlewood, Geoffrey P.

AU - Gilbert, Harry J.

PY - 1995/2/23

Y1 - 1995/2/23

N2 - Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.

AB - Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.

KW - (Pesudomonas)

KW - Esterase

KW - Ferulic acid

KW - Oligosaccharide

UR - http://www.scopus.com/inward/record.url?scp=0028860170&partnerID=8YFLogxK

U2 - 10.1016/0304-4165(94)00140-S

DO - 10.1016/0304-4165(94)00140-S

M3 - Article

C2 - 7873572

AN - SCOPUS:0028860170

SN - 0304-4165

VL - 1243

SP - 265

EP - 269

JO - BBA - General Subjects

JF - BBA - General Subjects

IS - 2

ER -

Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa

Abstract

Keywords

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