Fungi have been assured to be one of the wealthiest pools of bio-metabolites with remarkable potential for discovering new drugs. The pathogenic fungi, Fusarium oxysporum affects many valuable trees and crops all over the world, producing wilt. This fungus is a source of different enzymes that have variable industrial and biotechnological applications. Additionally, it is widely employed for the synthesis of different types of metal nanoparticles with various biotechnological, pharmaceutical, industrial, and medicinal applications. Moreover, it possesses a mysterious capacity to produce a wide array of metabolites with a broad spectrum of bioactivities such as alkaloids, jasmonates, anthranilates, cyclic peptides, cyclic depsipeptides, xanthones, quinones, and terpenoids. Therefore, this review will cover the previously reported data on F. oxysporum, especially its metabolites and their bioactivities, as well as industrial relevance in biotechnology and nanotechnology in the period from 1967 to 2021. In this work, 180 metabolites have been listed and 203 references have been cited.

Bright Side of Fusarium oxysporum: Secondary Metabolites Bioactivities and Industrial Relevance in Biotechnology and Nanotechnology.

In recent years, docosahexaenoic acid-containing phospholipids (DHA-PLs) have attracted much attention because of theirs unique health benefits. Compared with other forms of docosahexaenoic acid (DHA), DHA-PLs possess superior biological effects (e.g., anticancer, lipid metabolism regulation, visual development, and brain and nervous system biochemical reactions), more intricate metabolism mechanisms, and a stronger attraction to consumer. The production of DHA-PLs is hampered by several challenges associated with the limited content of DHA-PLs in natural sources, incomplete utilization of by-products, few microorganisms for DHA-PLs production, high cost, and complex process of artificial preparation of DHA-PLs. In this article, the sources, biological activities, and commercial applications of DHA-PLs were summarized, with intensive discussions on advantages of DHA-PLs over DHA, isomerism of DHA in phospholipids (PLs), and brain health. The excellent biological characteristics of DHA-PLs are primarily concerned with DHA and PLs. The metabolic fate of different DHA-PLs varies from the position of DHA in PLs to polar groups in DHA-PLs. Overall, well understanding of DHA-PLs about their sources and characteristics is critical to accelerate the production of DHA-PLs, economically enhance the value of DHA-PLs, and improve the applicability of DHA-PLs and the acceptance of consumers.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/1541-4337.12543

Advances in exogenous docosahexaenoic acid‐containing phospholipids: Sources, positional isomerism, biological activities, and advantages

A novel process for phosphatidylserine production using a Pichia pastoris whole-cell biocatalyst with overexpression of phospholipase D from Streptomyces halstedii in a purely aqueous system.

Advances in enzyme biocatalysis for the preparation of functional lipids.

Penicillium cyclopium lipase I (PCL) is a thermolabile triacylglycerol lipase with very low activity against monoacylglycerols, and there have been no reports on the transesterification of oil to produce biodiesel. A mutant PCLG47I with an improved thermostability was previously obtained through replacing Gly47 with Ile in PCL. In this study, a novel Pichia pastoris whole-cell biocatalyst (WCB) with overexpression of PCLG47I was constructed and characterized for biodiesel production from soybean oil. The optimum conditions for biodiesel preparation were 1 g soybean oil, 1 : 2 initial oil/methanol molar ratio with 3 times methanol addition of 1 : 0.75 oil/methanol molar ratio at 4 h intervals, 7% water content, 400 U lipase, temperature of 25 °C, and reaction time of 20 h. Under the optimum conditions, the FAME yield reached 60.7% and remained 47.3% after 4 batch cycles, and no glycerol was generated as a byproduct. These findings indicated that this WCB is a promising biocatalyst for biodiesel production in a relatively cost-effective manner. Additionally, the resulting enzymatic process may provide a potential method for biodiesel production at an industrial scale.

/pdf/development-of-a-pichia-pastoris-whole-cell-biocatalyst-with-xnojafqwaa.pdf

Development of a Pichia pastoris whole-cell biocatalyst with overexpression of mutant lipase I PCLG47I from Penicillium cyclopium for biodiesel production

Characterization of the recombinant porcine pancreas phospholipase A2 expressed in Pichia pastoris GS115 and its application to synthesis of 2-DHA-PS

l-alpha-glycerylphosphorylcholine (GPC) has been shown to enhance cognitive performance. Meanwhile, vegetable oils must be refined to remove the impurities for them to be edible. Phospholipase B (PLB), having the ability of hydrolyzing both the sn-1 and sn-2 acyl ester bonds of phospholipids, can produce GPC using PC as substrate and transform the non-hydratable phospholipids into their hydratable forms. The Saccharomyces cerevisiae plb gene, which encodes PLB, was cloned and expressed in Pichia pastoris GS115 to produce recombinant PLB (rPLB). Fermentation optimisation yielded rPLB activity levels as high as 1723 U/mL. rPLB demonstrated maximum enzymatic activity at 40 °C and pH 5.5 and was stable at temperatures between 30 and 40 °C and pH values between 5.0 and 6.0. rPLB synthesised GPC with a conversion rate of 17% (w/w) and exhibited high degumming activity towards peanut oil, decreasing the phosphorus content from 91.8 to 3.7 mg/kg within 3 h. This study describes a candidate phospholipase f...

https://www.tandfonline.com/doi/pdf/10.1080/13102818.2018.1455536

Cloning, expression and characterisation of phospholipase B from Saccharomyces cerevisiae and its application in the synthesis of l-alpha-glycerylphosphorylcholine and peanut oil degumming

A mutational laccase gene MLcc1 was synthesized with modified codons, based on the codon bias of Pichia pastoris, in order to improve the thermal stability of Trametes versicolor laccase. The mutant gene was subcloned into the expression vector pGAPZαA and was transformed into P. pastoris strain X33. The mature protein consisted of 498 amino acids and contained a changed aspartate with proline at the 14th position of the native laccase (NLCC1). Under optimum conditions, the laccase activity reached 194.06 U/L after 54 h by high cell density fermentation in a 5 L fermenter. After incubation at pH 4.6 for 2 h, the recombinant enzyme MLCC1 retained 54.9% of its maximum activity, whereas the wild-type enzyme retained about 50% of its maximum activity. More than 20% of the residual activity was detected after up to 120 min at 90 °C for MLCC1, whereas less than 10% of the activity was retained for NLCC1.

https://tandfonline.com/doi/pdf/10.1080/13102818.2015.1134278

Functional expression of Trametes versicolor thermotolerant laccase variant in Pichia pastoris

A rapid spectrophotometric method for the quantitative and quantitative detection of total coliforms

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Characterization of the recombinant porcine pancreas phospholipase A2 expressed in Pichia pastoris GS115 and its application to synthesis of 2-DHA-PS

Cloning, expression and characterisation of phospholipase B from Saccharomyces cerevisiae and its application in the synthesis of l-alpha-glycerylphosphorylcholine and peanut oil degumming

Functional expression of Trametes versicolor thermotolerant laccase variant in Pichia pastoris

A rapid spectrophotometric method for the quantitative and quantitative detection of total coliforms