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A Low-Temperature-Active Alkaline Pectate Lyase from Xanthomonas campestris ACCC 10048 with High Activity over a Wide pH Range

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Abstract

Alkaline pectate lyases are favorable for the textile industry. Here, we report the gene cloning and expression of a low-temperature-active alkaline pectate lyase (PL D) from Xanthomonas campestris ACCC 10048. Deduced PL D consists of a putative 27-residue signal peptide and a catalytic domain of 320 residues belonging to family PF09492. Recombinant PL D (r-PL D) produced in Escherichia coli was purified to electrophoretic homogeneity with a single step of Ni2+–NTA affinity chromatography and showed an apparent molecular weight of ~38 kDa. The pH and temperature optima of r-PL D were found to be 9.0 °C and 30 °C, respectively. Compared with its microbial counterparts, r-PL D had higher activity over a wide pH range (>45 % of the maximum activity at pH 3.0–12.0) and at lower temperatures (>35 % of activity even at 0 °C). The K m and V max values of r-PL D for polygalacturonic acid were 4.9 g l−1 and 30.1 μmol min−1 mg−1, respectively. Compared with the commercial compound pectinase from Novozymes, r-PL D showed similar efficacy in reducing the intrinsic viscosity of polygalacturonic acid (35.1 % vs. 36.5 %) and in bioscouring of jute (10.25 % vs. 10.82 %). Thus, r-PL D is a valuable additive candidate for the textile industry.

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Acknowledgments

This research was supported by the National Science and Technology Support Program (2011BADB02) and the National “948” Project (2011-G7-4) and the China Modern Agriculture Research System (CARS-42).

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Authors and Affiliations

  1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing, 100081, People’s Republic of China

    Peng Yuan, Kun Meng, Yaru Wang, Huiying Luo, Pengjun Shi, Huoqing Huang, Tao Tu, Peilong Yang & Bin Yao

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  1. Peng Yuan
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  2. Kun Meng
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  3. Yaru Wang
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  4. Huiying Luo
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  5. Pengjun Shi
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  6. Huoqing Huang
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  7. Tao Tu
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  8. Peilong Yang
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  9. Bin Yao
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Corresponding author

Correspondence to Bin Yao.

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Peng Yuan and Kun Meng contributed equally to this paper.

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Yuan, P., Meng, K., Wang, Y. et al. A Low-Temperature-Active Alkaline Pectate Lyase from Xanthomonas campestris ACCC 10048 with High Activity over a Wide pH Range. Appl Biochem Biotechnol 168, 1489–1500 (2012). https://doi.org/10.1007/s12010-012-9872-8

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  • DOI: https://doi.org/10.1007/s12010-012-9872-8

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