Biocompatibility of Brazilian native yeast-derived sophorolipids and Trichoderma harzianum as plant-growth promoting bioformulations.

The replacement of agrochemicals by biomolecules is imperative to mitigate soil contamination and inactivation of its core microbiota. Within this context, this study aimed at the interaction between a biological control agent such as Trichoderma harzianum CCT 2160 (BF-Th) and the biosurfactants (BSs) derived from the native Brazilian yeast Starmerella bombicola UFMG-CM-Y6419. Thereafter, their potential in germination of Oryza sativa L. seeds was tested. Both bioproducts were produced on site and characterized according to their chemical composition by HPLC-MS and GC-MS for BSs and SDS-PAGE gel for BF-Th. The BSs were confirmed to be sophorolipids (SLs) which is a well-studied compound with antimicrobial activity. The biocompatibility was examined by cultivating the fungus with SLs supplementation ranging from 0.1 to 2 g/L in solid and submerged fermentation. In solid state fermentation the supplementation of SLs enhanced spore production, conferring the synergy of both bioproducts. For the germination assays, bioformulations composed of SLs, BF-Th and combined (SLT) were applied in the germination of O. sativa L seeds achieving an improvement of up to 30% in morphological aspects such as root and shoot size as well as the presence of lateral roots. It was hypothesized that SLs were able to regulate phytohormones expression such as auxins and gibberellins during early stage of growth, pointing to their novel plant-growth stimulating properties. Thus, this study has pointed to the potential of hybrid bioformulations composed of biosurfactants and active endophytic fungal spores in order to augment the plant fitness and possibly the control of diseases.

Production and applications of pullulan from lignocellulosic biomass: Challenges and perspectives.

Pullulan is an exopolysaccharide produced by Aureobasidium pullulans, with interesting characteristics which lead to its application in industries such as pharmaceuticals, cosmetics, food, and others. To reduce production costs for industrial applications, cheaper raw materials such as lignocellulosic biomass can be utilized as a carbon and nutrient source for the microbial process. In this study, a comprehensive and critical review was conducted, encompassing the pullulan production process and the key influential variables. The main properties of the biopolymer were presented, and different applications were discussed. Subsequently, the utilization of lignocellulosics for pullulan production within the framework of a biorefinery concept was explored, considering the main published works that deal with materials such as sugarcane bagasse, rice husk, corn straw, and corn cob. Next, the main challenges and future prospects in this research area were highlighted, indicating the key strategies to favor the industrial production of pullulan from lignocellulosic biomasses.

Current applications and different approaches for microbial L-asparaginase production

ABSTRACT L-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in L-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, L-asparaginase catalyzes the hydrolysis of L-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of L-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents L-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

Current applications and different approaches for microbial L-asparaginase production

L-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in L-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, L-asparaginase catalyzes the hydrolysis of L-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of L-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents L-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.(AU)

Current applications and different approaches for microbial l-asparaginase production.

l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

Current applications and different approaches for microbial L-asparaginase production

ABSTRACT L-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in L-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, L-asparaginase catalyzes the hydrolysis of L-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of L-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents L-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.