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An effective degumming enzyme from Bacillus sp. Y1 and synergistic action of hydrogen peroxide and protease on enzymatic degumming of ramie fibers.

ABSTRACT: Enzymatic degumming, as an alternative to chemical processing, has attracted wide attention. However, to date, little information about other enzyme components with effective degumming except pectinase has been reported, and there is no report about the effect of bleaching agent (H2O2) on enzymatic degumming and combining enzymatic degumming and H2O2 bleaching process. In this study, we found that the crude enzyme of wild-type Bacillus sp. Y1 had a powerful and fast degumming ability. Its PGL activity was the highest at pH 9.6-10.0 and 60 °C and stable at pH 7-10.5 and 30-50 °C, having a wide scope of pH and temperature. Its PGL also had a high H2O2 tolerance, and the gum loss and brightness of fibers could be significantly improved when H2O2 was added into it for degumming. The synergistic action was also found between it and H2O2 on the degumming and bleaching of ramie fibers. All showed that it was very suitable for a joint process of enzymatic degumming and H2O2 bleaching. It also contained more proteins compared with a control pectinase, and its high protease content was further substantiated as a factor for effective degumming. Protease and pectinase also had a synergistic action on degumming.

SUBMITTER: Guo F

PROVIDER: S-EPMC3613079 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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An effective degumming enzyme from Bacillus sp. Y1 and synergistic action of hydrogen peroxide and protease on enzymatic degumming of ramie fibers.

Guo Fenfen F Zou Mouyong M Li Xuezhi X Zhao Jian J Qu Yinbo Y

BioMed research international 20130317

Enzymatic degumming, as an alternative to chemical processing, has attracted wide attention. However, to date, little information about other enzyme components with effective degumming except pectinase has been reported, and there is no report about the effect of bleaching agent (H2O2) on enzymatic degumming and combining enzymatic degumming and H2O2 bleaching process. In this study, we found that the crude enzyme of wild-type Bacillus sp. Y1 had a powerful and fast degumming ability. Its PGL ac ...[more]

PMID: 23586022

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Project description:BackgroundThe conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption. Pectate lyase PEL168 from Bacillus subtilis has been previously characterized and the protein structure was resolved. However, Bacillus is not a suitable host for pectate lyases during the degumming process since most Bacillus produce cellulases endogenously with a detrimental effect to the fiber. Pichia pastoris, which does not express endogenous cellulases and has high secretion capability, will be an ideal host for the expression. No previous work was reported concerning the heterologous expression of pectate lyase PEL168 in P. pastoris with an aim for industrial application in ramie bio-degumming.ResultsThe gene pel168 was expressed in P. pastoris in this study. The recombinant protein PEL168 in P. pastoris (PEL168P) showed two bands of 48.6 kDa and 51.4 kDa on SDS-PAGE whereas the enzyme expressed in E. coli (PEL168E) was the same as predicted with a band of 46 kDa. Deglycosylation digestion suggested that PEL168P was glycosylated. The optimum reaction temperature of the two PEL168s was 50°C, and the optimum pH 9.5. After preincubation at 60°C for 20 min, PEL168E completely lost its activity, whereas PEL168P kept 26% of the residual activity. PEL168P had a specific activity of 1320 U/mg with a Km of 0.09 mg/ml and a Vmax of 18.13 μmol/min. K⁺, Li⁺, Ni²⁺ and Sr²⁺ showed little or no inhibitory effect on PEL168P activity, and Ca²⁺ enhanced enzyme activity by 38%. PEL168P can remove the pectin from ramie effectively in a degumming process. A 1.5 fold increase of PEL168 enzyme expression in P. pastoris was achieved by further codon optimization.ConclusionsPectate lyase PEL168 with an available protein structure can be heterologously expressed in P. pastoris. The characterized recombinant PEL168P can be used to remove pectin from ramie efficiently and the expression level of PEL168 in P. pastoris was increased markedly by codon optimization. Therefore, PEL168 is an ideal candidate for further optimization and engineering for bio-degumming.

Dataset Information

An effective degumming enzyme from Bacillus sp. Y1 and synergistic action of hydrogen peroxide and protease on enzymatic degumming of ramie fibers.

Publications

An effective degumming enzyme from Bacillus sp. Y1 and synergistic action of hydrogen peroxide and protease on enzymatic degumming of ramie fibers.

Similar Datasets

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