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Microbial biosynthesis has become the leading commercial approach for large-scale production of terpenoids, a valuable class of natural products. Enhancing terpenoid production, however, requires complex modifications on the host organism. Recently, a two-step isopentenol utilization (IU) pathway relying solely on ATP as the cofactor has been proposed as an alternative to the mevalonate (MVA) pathway, streamlining the synthesis of the common terpenoid precursors. Herein, we find that isopentenol inhibits energy metabolism, leading to reduced efficiency of the IU pathway in Saccharomyces cerevisiae . To overcome this, we engineer an IU pathway-dependent (IUPD) strain, designed for growth-coupled production. The IUPD strain is compelled to enhance the ATP supply, essential for the IU pathway, and incorporates a high-throughput screening method for enzyme evolution. The refined IU pathway surpasses the MVA pathway in synthesizing complex terpenoids. Our work offers valuable insights into developing growth-coupled strains adapted to efficient natural product synthesis. The isopentenol utilization (IU) pathway has been reported as an alternative synthetic route for terpenoid synthesis, but isopentenol inhibits energy metabolism in baker’s yeast. Here, the authors solve the problem by replacing the mevalonate pathway with the IU pathway for growth-coupled squalene, β-carotene, and limonene production.

Deep eutectic solvents (DESs) are eutectic mixtures of salts and hydrogen bond donors with melting points low enough to be used as solvents. DESs have proved to be a good alternative to traditional organic solvents and ionic liquids (ILs) in many biocatalytic processes. Apart from the benign characteristics similar to those of ILs (e.g., low volatility, low inflammability and low melting point), DESs have their unique merits of easy preparation and low cost owing to their renewable and available raw materials. To better apply such solvents in green and sustainable chemistry, this review firstly describes some basic properties, mainly the toxicity and biodegradability of DESs. Secondly, it presents several valuable applications of DES as solvent/co-solvent in biocatalytic reactions, such as lipase-catalyzed transesterification and ester hydrolysis reactions. The roles, serving as extractive reagent for an enzymatic product and pretreatment solvent of enzymatic biomass hydrolysis, are also discussed. Further understanding how DESs affect biocatalytic reaction will facilitate the design of novel solvents and contribute to the discovery of new reactions in these solvents.

Odd-chain fatty acids (OCFAs) naturally occur in bacteria, higher animals, and in plants. During recent years, they have received increasing attention due to their unique pharmacological properties and usefulness for agricultural and industrial applications. Recently, OCFAs have been identified and quantified in a few organisms, and new pharmacological functions of OCFAs have been reported. Some of the publications are related to the optimization of OCFA production through fermentation and genetic engineering. The present review aims to provide a summary on the recent progress in the field of microbial-derived OCFAs. More specifically, we outline the publications of OCFAs related to (i) different sources of OCFAs; (ii) endogenous synthesis of OCFAs; (iii) production of OCFAs through fermentation; (iv) genetic engineering related to OCFA; and (v) role of OCFAs in human health and disease. Finally, some areas that require further research are discussed.

Pullulanase (EC 3.2.1.41) is a starch-debranching enzyme in the α-amylase family and specifically cleaves α-1,6-glycosidic linkages in starch-type polysaccharides, such as pullulan, β-limited dextrin, glycogen, and amylopectin. It plays a key role in debranching and hydrolyzing starch completely, thus bring improved product quality, increased productivity, and reduced production cost in producing resistant starch, sugar syrup, and beer. Plenty of researches have been made with respects to the discovery of either thermophilic or mesophilic pullulanases, however, few examples meet the demand of industrial application. This review presents the progress made in the recent years from the first aspect of characteristics of pullulanases. The heterologous expression of pullulanases in different microbial hosts and the methods used to improve the expression effectiveness and the regulation of enzyme production are also described. Then, the function evolution of pullulanases from a protein engineering view is discussed. In addition, the immobilization strategy using novel materials is introduced to improve the recyclability of pullulanases. At the same time, we indicate the trends in the future research to facilitate the industrial application of pullulanases.

Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading (82.2 mg enzyme/g) and activity recovery (95.9%). Compared with free PCL, PCL@MCNC exhibited significantly enhanced stability and solvent tolerance, due to the increase of enzyme structure rigidity. The observable optimum pH and temperature for PCL@MCNC were higher than those of free PCL. PCL@MCNC manifested relatively higher enzyme-substrate affinity and catalytic efficiency. Moreover, PCL@MCNC was capable of effectively catalyzing asymmetric hydrolysis of ketoprofenethyl ester with high yield of 43.4% and product e.e. of 83.5%. Besides, immobilization allowed PCL@MCNC reuse for at least 6 consecutive cycles retaining over 66% of its initial activity. PCL@MCNC was readily recycled by magnetic forces. Remarkably, the as-prepared nanobiocatalyst PCL@MCNC is promising for biocatalysis.

A copper analogue of Prussian blue incorporated multienzyme system was successfully established via a biomimetic mineralization process, whereas CPB with peroxidase-like activity provided protecting effect for encapsulated glucose oxidase from attack in hostile conditions. The hybrid composite was developed as a colorimetric biosensor for ultrasensitive detection of glucose, with a low detection limit (0.48 μM).Graphic Abstract

Probiotics have been widely explored for their potential in managing hyperuricemia. However, their isolation and identification are fundamental prerequisites for practical application. In this study, 254 lactic acid bacteria (LAB) strains were isolated from Chinese sauerkraut and screened for probiotic potential based on genomic and phenotypic characteristics, as well as nucleoside-degrading activity relevant to decrease serum urate. Among them, Lactiplantibacillus plantarum (L. plantarum) F42 exhibited the highest bile salt tolerance (survivor rate: 19.46 ± 4.33%), strong adhesion to Caco-2 cells (1.89 ± 0.12%), effective nucleoside degradation (inosine: 5.46 ± 0.67 mg∙L−1∙min−1; guanosine: 3.84 ± 0.11 mg∙L−1∙min−1), and notable anti-listeria activity (inhibition zone: 6.9 ± 0.3 mm). Based on its functional profile, L. plantarum F42 was selected as a promising probiotic candidate for further investigation of its urate-lowering effects. This work provides a new insight into anti-hyperuricemia probiotic selection based on in vitro nucleoside-degrading activity.

Papain (PA) immobilized onto magnetic nanocrystalline cellulose (PA@MNCC) was successfully fabricated and adopted as an efficient biocatalyst for the synthesis of N-(benzyloxycarbonyl)-alanyl-histidine (Z-Ala-His) dipeptide. Introducing deep eutectic solvents (DESs) as reaction media promoted the synthesis of the Z-Ala-His dipeptide. The effects of reaction conditions on the yield of papain catalytic Z-Ala-His were systematically investigated with the highest yield of 68.4%, which was higher than free papain (63.3%). Besides, this novel PA@MNCC composite can be easily recycled from the reaction system by magnetic forces. In a word, the PA@MNCC composite exhibited great potential for efficient biosynthesis of dipeptide in DESs.

In the study, monodispersed silver nanoparticles (AgNPs) with an average diameter of 9.57 nm were efficiently and controllably biosynthesized by a reductase from Fusarium solani DO7 only in the presence of β-NADPH and polyvinyl pyrrolidone (PVP). The reductase responsible for AgNP formation in F. solani DO7 was further confirmed as 1,4-α-glucosidase. Meanwhile, based on the debate on the antibacterial mechanism of AgNPs, this study elucidated in further depth that antibacterial action of AgNPs was achieved by absorbing to the cell membrane and destabilizing the membrane, leading to cell death. Moreover, AgNPs could accelerate the catalytic reaction of 4−nitroaniline, and 86.9% of 4-nitroaniline was converted to p-phenylene diamine in only 20 min by AgNPs of controllable size and morphology. Our study highlights a simple, green, and cost-effective process for biosynthesizing AgNPs with uniform sizes and excellent antibacterial activity and catalytic reduction of 4-nitroaniline.

The extraction conditions and antioxidant activities of rutin from Sophora japonica bud by deep eutectic solvents were investigated. Box–Behnken design was used to optimize the extraction conditions and the scavenging activities of DPPH, O2− and ·OH of purified rutin were evaluated. The highest yield of 279.8 mg/g was achieved in the extraction medium of choline chloride/triethlene glycol (1/4) under the optimum conditions: water content of the DES 18.1%, extraction time 28.3 min, extraction temperature 70 °C and liquid–solid ratio 10 mg/1 g. The highest extraction amount was slightly different from the predicted value of the established second-order polynomial equation. In addition, The EC50 of DPPH scavenging, O2− scavenging and ·OH scavenging of rutin were 5.68 µg/mL, 0.19 and 0.28 mg/mL, respectively. The above results indicate rutin extracted by the choline chloride/triethylene glycol has excellent antioxidant activity and was an admirable free radical scavenger.