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Title: Temperature sensitivity of mineral-enzyme interactions on the hydrolysis of cellobiose and indican by β-glucosidase

Abstract

Extracellular enzymes are essentially responsible for depolymerizing soil organic matter (SOM) in terrestrial ecosystems, and soil minerals are known to affect enzyme activity. Yet, the mechanisms and the effects of mineral-enzyme interactions on enzymatic degradation of organic matter remain poorly understood. In this study, we examined the adsorption of fungal β-glucosidase enzyme on minerals and time-dependent changes of enzymatic reactivity, measured by the degradation of two organic substrates (i.e., cellobiose and indican) under both cold (4°C) and warm (20 and 30°C) conditions. Hematite, kaolinite, and montmorillonite were used, to represent three common soil minerals with distinctly different surface charges and characteristics. β-glucosidase was found to sorb more strongly onto hematite and kaolinite than montmorillonite. All three minerals inhibited enzyme degradation of cellobiose and indican, likely due to the inactivation or hindrance of enzyme active sites. The mineral-bound β-glucosidase retained its specificity for organic substrate degradation, and increasing temperature from 4 to 30°C enhanced the degradation rates by 2–4 fold for indican and 5–9 fold for cellobiose. These results suggest that enzyme adsorption, mineral type, temperature, and organic substrate specificity are important factors influencing enzymatic reactivity and thus have important implications in further understanding and modeling complex enzyme-facilitated SOM transformations inmore » terrestrial ecosystems.« less

Authors:
ORCiD logo [1];  [2];  [2];  [1];  [2];  [2];  [3]; ORCiD logo [4]; ORCiD logo [4]; ORCiD logo [4]
  1. Oakland Univ., Rochester, MI (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  2. Oakland Univ., Rochester, MI (United States)
  3. Huazhong Agricultural Univ., Wuhan (China)
  4. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Science Foundation (NSF)
OSTI Identifier:
1530080
Grant/Contract Number:  
AC05-00OR22725; CBET-1841301
Resource Type:
Accepted Manuscript
Journal Name:
Science of the Total Environment
Additional Journal Information:
Journal Volume: 686; Journal Issue: C; Journal ID: ISSN 0048-9697
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Mineral; Enzyme; Adsorption; Soil organic matter degradation; Temperature sensitivity

Citation Formats

Yang, Ziming, Liao, Yiju, Fu, Xuan, Zaporski, Jared, Peters, Stephanie, Jamison, Megan, Liu, Yurong, Wullschleger, Stan D., Graham, David E., and Gu, Baohua. Temperature sensitivity of mineral-enzyme interactions on the hydrolysis of cellobiose and indican by β-glucosidase. United States: N. p., 2019. Web. doi:10.1016/j.scitotenv.2019.05.479.
Yang, Ziming, Liao, Yiju, Fu, Xuan, Zaporski, Jared, Peters, Stephanie, Jamison, Megan, Liu, Yurong, Wullschleger, Stan D., Graham, David E., & Gu, Baohua. Temperature sensitivity of mineral-enzyme interactions on the hydrolysis of cellobiose and indican by β-glucosidase. United States. doi:10.1016/j.scitotenv.2019.05.479.
Yang, Ziming, Liao, Yiju, Fu, Xuan, Zaporski, Jared, Peters, Stephanie, Jamison, Megan, Liu, Yurong, Wullschleger, Stan D., Graham, David E., and Gu, Baohua. Sat . "Temperature sensitivity of mineral-enzyme interactions on the hydrolysis of cellobiose and indican by β-glucosidase". United States. doi:10.1016/j.scitotenv.2019.05.479.
@article{osti_1530080,
title = {Temperature sensitivity of mineral-enzyme interactions on the hydrolysis of cellobiose and indican by β-glucosidase},
author = {Yang, Ziming and Liao, Yiju and Fu, Xuan and Zaporski, Jared and Peters, Stephanie and Jamison, Megan and Liu, Yurong and Wullschleger, Stan D. and Graham, David E. and Gu, Baohua},
abstractNote = {Extracellular enzymes are essentially responsible for depolymerizing soil organic matter (SOM) in terrestrial ecosystems, and soil minerals are known to affect enzyme activity. Yet, the mechanisms and the effects of mineral-enzyme interactions on enzymatic degradation of organic matter remain poorly understood. In this study, we examined the adsorption of fungal β-glucosidase enzyme on minerals and time-dependent changes of enzymatic reactivity, measured by the degradation of two organic substrates (i.e., cellobiose and indican) under both cold (4°C) and warm (20 and 30°C) conditions. Hematite, kaolinite, and montmorillonite were used, to represent three common soil minerals with distinctly different surface charges and characteristics. β-glucosidase was found to sorb more strongly onto hematite and kaolinite than montmorillonite. All three minerals inhibited enzyme degradation of cellobiose and indican, likely due to the inactivation or hindrance of enzyme active sites. The mineral-bound β-glucosidase retained its specificity for organic substrate degradation, and increasing temperature from 4 to 30°C enhanced the degradation rates by 2–4 fold for indican and 5–9 fold for cellobiose. These results suggest that enzyme adsorption, mineral type, temperature, and organic substrate specificity are important factors influencing enzymatic reactivity and thus have important implications in further understanding and modeling complex enzyme-facilitated SOM transformations in terrestrial ecosystems.},
doi = {10.1016/j.scitotenv.2019.05.479},
journal = {Science of the Total Environment},
number = C,
volume = 686,
place = {United States},
year = {2019},
month = {6}
}

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