Biotechnological Advances in Industrial Enzymes and Green Bioprocessing

A special issue of Bioengineering (ISSN 2306-5354). This special issue belongs to the section "Biochemical Engineering".

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 2843

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Guest Editor
National Center of Technology Innovation for Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China
Interests: gene mining for novel enzymes; enzyme engineering for bio-manufacturing; efficiency expression of enzymes; develop novel industrial microorganisms; develop green bioprocessing

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Guest Editor
School of Life Sciences and Department Chemical Engineering, Tsinghua University, Beijing 100084, China
Interests: synthetic biology; microbial metabolic engineering; biological materials; industrial biotechnology
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Guest Editor
School of Life Science and Biopharmaceutics, Shenyang Pharmaceutical University, Shenyang 110016, China
Interests: synthetic biology; metabolic engineering; biosynthesis of microbial metabolites; directed evolution

Special Issue Information

Dear Colleagues,

The green bio-manufacturing industry, characterized by high efficiency, safety, energy-saving capability, and environmental-friendliness, is a global hot spot in industrial development with broad market prospects. Industrial enzymes represent the “chip” of green biological process. The exploitation, molecular modification, high-efficiency expression and application of new industrial enzymes constitute the enabling technologies of green bio-manufacturing. At present, along with the rapid development of the key techniques of synthetic biology such as genome editing and metabolic engineering, more and more industrial microorganisms are being designed and modified for green bio-manufacturing. This Special Issue of Bioengineering, entitled “Biotechnological advances in industrial enzymes and green bioprocessing”, addresses worldwide advances in biotechnology and bioengineering for promoting the rapid development of industrial enzymes and green bioprocessing in food industry, feed industry, agricultural field, pharmaceuticals industry, traditional light industries and other domains.

Dr. Hongchen Zheng
Prof. Dr. Guo-Qiang Chen
Dr. Xianpu Ni
Guest Editors

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Keywords

  • biotechnology
  • bioengineering
  • industrial enzyme
  • enzyme engineering
  • protein expression system
  • green bioprocessing
  • industrial microorganism
  • synthetic biology
  • engineering strain
  • metabolic engineering

Published Papers (2 papers)

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Research

12 pages, 2272 KiB  
Article
Trehalose Production Using Three Extracellular Enzymes Produced via One-Step Fermentation of an Engineered Bacillus subtilis Strain
by Xi Sun, Jun Yang, Xiaoping Fu, Xingya Zhao, Jie Zhen, Hui Song, Jianyong Xu, Hongchen Zheng and Wenqin Bai
Bioengineering 2023, 10(8), 977; https://doi.org/10.3390/bioengineering10080977 - 18 Aug 2023
Cited by 1 | Viewed by 1221
Abstract
At present, the double-enzyme catalyzed method using maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase) is the mainstream technology for industrial trehalose production. However, MTSase and MTHase are prepared mainly using the heterologous expression in the engineered Escherichia coli strains so far. In this [...] Read more.
At present, the double-enzyme catalyzed method using maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase) is the mainstream technology for industrial trehalose production. However, MTSase and MTHase are prepared mainly using the heterologous expression in the engineered Escherichia coli strains so far. In this study, we first proved that the addition of 3 U/g neutral pullulanase PulA could enhance the trehalose conversion rate by 2.46 times in the double-enzyme catalyzed system. Then, a CBM68 domain was used to successfully assist the secretory expression of MTSase and MTHase from Arthrobacter ramosus S34 in Bacillus subtilis SCK6. At the basis, an engineered strain B. subtilis PSH02 (amyE::pulA/pHT43-C68-ARS/pMC68-ARH), which co-expressed MTSase, MTHase, and PulA, was constructed. After the 24 h fermentation of B. subtilis PSH02, the optimum ratio of the extracellular multi-enzymes was obtained to make the highest trehalose conversion rate of 80% from 100 g/L maltodextrin. The high passage stability and multi-enzyme preservation stability made B. subtilis PSH02 an excellent industrial production strain. Moreover, trehalose production using these extracellular enzymes produced via the one-step fermentation of B. subtilis PSH02 would greatly simplify the procedure for multi-enzyme preparation and be expected to reduce production costs. Full article
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13 pages, 2840 KiB  
Article
Cofactor Metabolic Engineering of Escherichia coli for Aerobic L-Malate Production with Lower CO2 Emissions
by Zhiming Jiang, Youming Jiang, Hao Wu, Wenming Zhang, Fengxue Xin, Jiangfeng Ma and Min Jiang
Bioengineering 2023, 10(8), 881; https://doi.org/10.3390/bioengineering10080881 - 25 Jul 2023
Cited by 1 | Viewed by 1182
Abstract
Escherichia coli has been engineered for L-malate production via aerobic cultivation. However, the maximum yield obtained through this mode is inferior to that of anaerobic fermentation due to massive amounts of CO2 emissions. Here, we aim to address this issue by reducing [...] Read more.
Escherichia coli has been engineered for L-malate production via aerobic cultivation. However, the maximum yield obtained through this mode is inferior to that of anaerobic fermentation due to massive amounts of CO2 emissions. Here, we aim to address this issue by reducing CO2 emissions of recombinant E. coli during aerobic L-malate production. Our findings indicated that NADH oxidation and ATP-synthesis-related genes were down-regulated with 2 g/L of YE during aerobic cultivations of E. coli E23, as compared to 5 g/L of YE. Then, E23 was engineered via the knockout of nuoA and the introduction of the nonoxidative glycolysis (NOG) pathway, resulting in a reduction of NAD+ and ATP supplies. The results demonstrate that E23 (ΔnuoA, NOG) exhibited decreased CO2 emissions, and it produced 21.3 g/L of L-malate from glucose aerobically with the improved yield of 0.43 g/g. This study suggests that a restricted NAD+ and ATP supply can prompt E. coli to engage in incomplete oxidization of glucose, leading to the accumulation of metabolites instead of utilizing them in cellular respiration. Full article
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