Nucleotide Sequence of the Pectate Lyase Gene from Alkali-tolerant<i>Bacillus</i>sp. YA-14

Kim, Jin Man; Park, Hee-Kyoung; Yum, Do-Young; Hahm, Byoung-Kwon; Bai, Dong-Hoon; Yu, Ju-Hyun

doi:10.1271/bbb.58.947

Cited by 3 publications

(1 citation statement)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The 14 mutations are of great value as a basis for the futher study of the differences between the two xylanases by structural analysis. As previously reported, XylX is a thermostable xylanase, the endo-1, 4β-xylanase and xylanase J are alkaliphilic xylanases, and all three xylanases belong to glycosyl hydrolase family 11 [8,11,16]. Thus, both sequence analysis and further characterization suggest that the purified XynG1-1 from P. campinasensis G1-1 is a thermostabe and alkaline-tolerant xylanase.…”

Section: Effects Of Various Metal Ions and Additives On Xylanase Actisupporting

confidence: 53%

Isolation, Purification, and Characterization of a Thermostable Xylanase from a Novel Strain, Paenibacillus campinasensis G1-1

Zheng

Liu²,

Liu³

et al. 2012

J. Microbiol. Biotechnol.

View full text Add to dashboard Cite

High levels of xylanase activity (143.98 IU/ml) produced by the newly isolated Paenibacillus campinasensis G1-1 were detected when it was cultivated in a synthetic medium. A thermostable xylanase, designated XynG1-1, from P. campinasensis G1-1 was purified to homogeneity by Octyl-Sepharose hydrophobic-interaction chromatography, Sephadex G75 gel-filter chromatography, and Q-Sepharose ion-exchange chromatography, consecutively. By multistep purification, the specific activity of XynG1-1 was up to 1,865.5 IU/mg with a 9.1-fold purification. The molecular mass of purified XynG1-1 was about 41.3 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Sequence analysis revealed that XynG1-1 containing 377 amino acids encoded by 1,134 bp genomic sequences of P. campinasensis G1-1 shared 96% homology with XylX from Paenibacillus campinasensis BL11 and 77%~78% homology with xylanases from Bacillus sp. YA-335 and Bacillus sp. 41M-1, respectively. The activity of XynG1-1 was stimulated by Ca 2+ , Ba 2+ , DTT, and βmercaptoethanol, but was inhibited by Ni 2+ , Fe 2+ , Fe 3+ , Zn 2+ , SDS, and EDTA. The purified XynG1-1 displayed a greater affinity for birchwood xylan, with an optimal temperature of 60 o C and an optimal pH of 7.5. The fact that XynG1-1 is cellulose-free, thermostable (stability at high temperature of 70 o C~80 o C), and active over a wide pH range (pH 5.0~9.0) suggests that the enzyme is potentially valuable for various industrial applications, especially for pulp bleaching pretreatment.

show abstract

Section: Effects Of Various Metal Ions and Additives On Xylanase Actisupporting

confidence: 53%

Isolation, Purification, and Characterization of a Thermostable Xylanase from a Novel Strain, Paenibacillus campinasensis G1-1

Zheng

Liu²,

Liu³

et al. 2012

J. Microbiol. Biotechnol.

View full text Add to dashboard Cite

show abstract

Cloning and expression of a pectate lyase gene from Bacillus alcalophillus NTT33

Zhai

Cao

Wang

2003

Enzyme and Microbial Technology

View full text Add to dashboard Cite

Characterization of Two Paenibacillus amylolyticus Strain 27C64 Pectate Lyases with Activity on Highly Methylated Pectin

Boland

Henriksen

Doran‐Peterson

2010

Appl Environ Microbiol

View full text Add to dashboard Cite

Two pectate lyases were identified from Paenibacillus amylolyticus 27C64; both enzymes demonstrated activity on methylated pectin in addition to polygalacturonic acid. PelA is in a subclass of the pectate lyase family III. PelB shows some features of pectate lyase family I but is highly divergent.Pectinases have many industrial applications, including uses in food and textile production (9, 12). Additionally, pectinases are important for the degradation of biomass, where pectin can comprise a significant portion of plant structure (5, 6). The degradation of pectin requires methylesterases and depolymerases. Pectin methylesterases are responsible for the hydrolysis of methylester linkages from the polygalacturonic acid (PGA) backbone (24), while pectin depolymerases act upon the polygalacturonate backbone and belong to one of two families, polygalacturonases or lyases. Polygalacturonases hydrolytically cleave the polygalacturonate chain, while lyases cleave by ␤-elimination, giving a ⌬4,5-unsaturated product (10, 19). There are two types of lyases: pectate lyases (PLs), which cleave unesterified polygalacturonate, and pectin lyases, which cleave methylesterified pectin.Paenibacillus amylolyticus strain 27C64, isolated from the larval hindgut of the aquatic crane fly, Tipula abdominalis, possesses a wide range of lignocellulose-degrading enzymes. This study describes two pectate lyases from P. amylolyticus that display unusual activity by combining traits of pectate and pectin lyases (2,7,21,22).Identification of pelA and pelB. A library containing 2-to

show abstract

Nucleotide Sequence of the Pectate Lyase Gene from Alkali-tolerantBacillussp. YA-14

Cited by 3 publications

References 1 publication

Isolation, Purification, and Characterization of a Thermostable Xylanase from a Novel Strain, Paenibacillus campinasensis G1-1

Isolation, Purification, and Characterization of a Thermostable Xylanase from a Novel Strain, Paenibacillus campinasensis G1-1

Cloning and expression of a pectate lyase gene from Bacillus alcalophillus NTT33

Characterization of Two Paenibacillus amylolyticus Strain 27C64 Pectate Lyases with Activity on Highly Methylated Pectin

Contact Info

Product

Resources

About