Systematic Unravelling of the Inulin Hydrolase from for Efficient Conversion of Inulin to Poly-(γ-glutamic Acid)

Overview

Journal Biotechnol Biofuels

Publisher Biomed Central

Specialty Biotechnology

Date 2019 Jun 19

PMID 31210783

Citations 5

Authors

Yibin Qiu

Yifan Zhu

Yatao Zhang

Yuanyuan Sha

Yijing Zhan

Zongqi Xu

Sha Li

Xiaohai Feng

Hong Xu

Affiliations

Soon will be listed here.

Abstract

Background: NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain NB.

Results: The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a / of (6.93 ± 0.27) × 10 for inulin; its enzymatic activity was stimulated by metal ions, like K, Mn, or Ca. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of gene suppressed inulin utilization by strain NB. Overexpression of significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption.

Conclusions: The inulin hydrolase CscA is critical for inulin metabolism in and indicates potential application in Jerusalem artichoke biorefinery.

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