Industrial biotechnology promises to make a significant contribution in enabling the sustainable development, and need the solid support from its basic discipline. As the basis of industrial biotechnology, industrial biology is to study the basic laws and mechanisms of biological behavior in industrial environment and to solve the key scientific problems for understanding, designing and constructing the organisms adapted to the application of industrial environment. In order to comprehend the status of industrial biology, we published this special issue to review the progress and trends of industrial biology from the three aspects of industrial protein science, cell science and fermentation science, respectively, for laying the foundation for the development of industrial biotechnology.
Biotechnology ; Fermentation ; Industrial Microbiology

Taiwanofungus camphoratus is a valuable and rare medicinal mushroom with various bioactivities, such as liver protection and anti-cancer. T. camphoratus can produce many arthroconidia at the end of submerged fermentation, but molecular mechanism underlying this submerged conidiation remains unknown. In this study, we found that Ca²⁺ concentration in culture medium significantly affected the arthroconidium production of T. camphoratus. Then, we identified two proteins (CaM and HSP90) involved in Ca²⁺/calmodulin signaling pathway and one protein (AbaA) involved in FluG-mediated conidiation pathway by two-dimensional electrophoresis analyses. Furthermore, we proposed a Ca²⁺/calmodulin- and FluG-mediated signaling pathway by bioinformatics analysis. By real-time quantitative PCR analyses of 23 key genes in the Ca²⁺/calmodulin- and FluG-mediated conidiation pathway, we found that expression levels of 7 genes (crz1, hsp90, flbB, brlA, abaA, wetA and fadA) showed significant responses to Ca²⁺ concentration in fermentation medium. Our research is beneficial for elucidating the underlying mechanism of submerged fermentation conidiation for T. camphoratus.

Objective To review and analyse the CT distinguishing features of pulmonary cryptococcosis (PC)for improving the level of image diagnosis of the disease.Methods CT images and clinical details of 19 patients with biopsy or surgery pathology con-firmed PC were reviewed and analysed.Results Nodules or masses were presented in 10 cases,in which most casescases were nod-ules,lesions ranged in diameter from 1 cm to 2.5 cm.Multiple nodules were easy to fuse.Consolidation were presented in 6 cases,with high attenuation and clear border.3 cases were mixed type,with nodule,mass consolidation and ground glass attenuation.The lesions were mostly located in the inferior lobes(47%)and peripheral lung(68%).The features of pleural thickening,air bronchus sign,halo sign and cavitations were observed in 42%,36%,26%,21% of patients respectively.Conclusion CT findings of PC are diversity.The lesions are mostly located in the inferior and peripheral lung.Lesions are mild to moderate enhanced.Pleural thickening,air bronchus sign,halo sign,cavitations will be useful for the diagnosis.

Xylanase is the key enzyme to degrade xylan that is a major component of hemicellulose. The enzyme has potential industrial applications in the food, feed, paper and flax degumming industries. The use of xylanases becomes more and more important in the paper industry for bleaching purposes. Xylanases used in the pulp bleaching process should be stable and active at high temperature and alkaline pH. Thermophilic and alkalophilic xylanases could be obtained by screening the wild type xylanases or engineering the mesophilic and neutral enzymes. In this paper, we reviewed recent progress of screening of the thermophilic and alkalophilic xylanases, molecular mechanism of thermal and alkaline adaptation and molecular engineering. Future research prospective was also discussed.
Endo-1,4-beta Xylanases ; chemistry ; Enzyme Stability ; Hot Temperature ; Hydrogen-Ion Concentration ; Paper ; Protein Engineering

Thermophilic and alkalophilic xylanases have great potential in the pulp bleaching industry. In order to improve the thermal stability of an alkaline family 11 xylanase Xyn11A-LC, aromatic residues were introduced into the N-terminus of the enzyme by rational design. The mutant increased the optimum temperature by 5 degrees C. The wild type had a half-time of 22 min at 65 degrees C and pH 8.0 (Tris-HCl buffer). Under the same condition, the mutant had the half-time of 106 min. CD spectroscopy revealed that the melting temperature (T(m)) values of the wild type and mutant were 55.3 degrees C and 67.9 degrees C, respectively. These results showed that the introduction of aromatic residues could enhance the thermal stability of Xyn11A-LC.
Endo-1,4-beta Xylanases ; chemistry ; Enzyme Stability ; Hydrogen-Ion Concentration ; Protein Engineering ; Temperature

5-aminolevulinic acid (ALA), a precursor for biosynthesis of pyrrole compounds in living organisms, has been widely used in agriculture and medical photodynamics therapy and is regarded as a promising value-added bio-based chemical. In the previous investigations on ALA production with recombinant Escherichia coli expressing heterogenous C4 pathway gene, LB media supplemented with glucose and ALA precursors succinate and glycine is widely used, leading to high production cost. Succinate participates in ALA biosynthesis in a form of succinyl-CoA. In this study, genes involved in succinyl-CoA consumption, sdhAB (encoding succinic dehydrogenase) or sucCD (encoding succinyl-CoA synthetase) of E. coli MG1655 was knocked out and tested for ALA accumulation. In comparison with the recombinant E. coli strain expressing heterogenous ALA synthetase, the sdhAB- or sucCD-deficient strain accumulate 25.59% and 12.40%, respectively, more ALA in a 5 L fermentor using a defined synthetic medium with glucose as main carbon source and without supplementation of succinate, providing a novel cost-effective approach for industrial production of ALA.
Aminolevulinic Acid ; metabolism ; Escherichia coli ; enzymology ; genetics ; metabolism ; Industrial Microbiology ; methods ; Metabolic Engineering ; methods ; Recombinant Proteins ; genetics ; metabolism ; Succinate Dehydrogenase ; genetics ; metabolism ; Succinate-CoA Ligases ; genetics ; metabolism

Adipic acid is a six-carbon dicarboxylic acid, mainly for the production of polymers such as nylon, chemical fiber and engineering plastics. Its annual demand is close to 3 million tons worldwide. Currently, the industrial production of adipic acid is based on the oxidation of aromatics from non-renewable petroleum resources by chemo-catalytic processes. It is heavily polluted and unsustainable, and the possible alternative method for adipic acid production should be developed. In the past years, with the development of synthetic biology and metabolic engineering, green and clean biotechnological methods for adipic acid production attracted more attention. In this study, the research advances of adipic acid and its precursor production are reviewed, followed by addressing the perspective of the possible new pathways for adipic acid production.
Adipates ; metabolism ; Bacteria ; genetics ; metabolism ; Fungi ; genetics ; metabolism ; Industrial Microbiology ; methods ; Metabolic Engineering ; methods ; Metabolic Networks and Pathways ; genetics

Lactic acid has a wide range of uses in the chemical, pharmaceutical and food industry. With rapid development of poly (lactic acid) industry, the demand for polymer-grade L-lactic acid is continuously increasing. Developing low-cost, non-food-biomass-lactic-acid fermentation process and the fermentation-separation coupled technology are trends to reduce polymer-grade L-lactic acid production cost. This review summarized the most recent advances in low-cost L-lactic acid fermentation based on the use of non-food biomass, followed by addressing the key issue that might be strategically important for future development of polymer-grade L-lactic acid production in industry.
Biomass ; Biotechnology ; trends ; Cellulose ; metabolism ; Fermentation ; Insulin ; metabolism ; Lactic Acid ; metabolism ; Manihot ; metabolism ; Polymers ; metabolism

Carbonyl reductases catalyze carbonyl compounds to chiral alcohols that are important building blocks in fine chemical industry. To study carbonyl reductase from Pichia pastoris GS115 (ppcr), we discovered a new gene (ppcr) encoding an NADPH-dependent carbonyl reductase by genomic data mining. It was amplified by PCR from the genomic DNA, and expressed in Escherichia coli BL21 (DE3). The recombinant protein was purified to homogeneity. The optimum temperature was 37 degrees C and the optimum pH of PPCR was 6.0. PPCR was stable below 45 degrees C. The Km and k(cat) value of the enzyme for ethyl 3-methyl-2-oxobutanoate were 9.48 mmol/L and 0.12 s, respectively. The enzyme had broad substrate specificity and high enantioselectivity. It catalyzed the reduction of aldehydes, a-ketoesters, beta-ketoesters and aryl ketones to give the corresponding alcohols with >97% ee with only a few exceptions, showing its application potential in the synthesis of chiral alcohols.
Alcohol Oxidoreductases ; biosynthesis ; chemistry ; genetics ; Amino Acid Sequence ; Biotechnology ; methods ; Cloning, Molecular ; Escherichia coli ; genetics ; metabolism ; Molecular Sequence Data ; Pichia ; enzymology ; Recombinant Proteins ; biosynthesis ; chemistry ; genetics ; Stereoisomerism ; Substrate Specificity ; Temperature

Asymmetric reduction of bulky diaryl ketones is still one of the challenging tasks in biocatalysis. By genomic data mining, a putative carbonyl reductase gene pascr was found in Pichia pastoris GS115. pascr was cloned and over-expressed in Escherichia coli Rosseta2 (DE3). The recombinant enzyme was purified to homogeneity by Ni-NTA column and its catalytic properties were studied. PasCR strictly used NADPH as cofactor, gel filtration and SDS-PAGE analysis suggested that the native form of PasCR was a dimmer. PasCR exhibited the highest activity at 35 degrees C in phosphate buffer at pH 6.5. The enzyme catalyzed the reduction of some bulky diaryl ketones, such as 4-methylbenzophenone, 2-methylbenzophenone and 4-chlorobenzophenone, especially for 4-methylbenzophenone, the product S--alcohol was obtained with 85% ee.
Alcohol Oxidoreductases ; genetics ; Amino Acid Sequence ; Catalysis ; Cloning, Molecular ; Ketones ; chemistry ; Molecular Sequence Data ; Pichia ; enzymology ; genetics ; Stereoisomerism