https://repositorio.unb.br/bitstream/10482/6389/1/ARTIGO_ApplicationMicrobialAmylase.pdf

Application of microbial α-amylase in industry - A review

Pullulan: Microbial sources, production and applications

Enzymes are the large biomolecules that are required for the numerous chemical interconversions that sustain life. They accelerate all the metabolic processes in the body and carry out a specific task. Enzymes are highly efficient, which can increase reaction rates by 100 million to 10 billion times faster than any normal chemical reaction. Due to development in recombinant technology and protein engineering, enzymes have evolved as an important molecule that has been widely used in different industrial and therapeutical purposes. Microbial enzymes are currently acquiring much attention with rapid development of enzyme technology. Microbial enzymes are preferred due to their economic feasibility, high yields, consistency, ease of product modification and optimization, regular supply due to absence of seasonal fluctuations, rapid growth of microbes on inexpensive media, stability, and greater catalytic activity. Microbial enzymes play a major role in the diagnosis, treatment, biochemical investigation, and monitoring of various dreaded diseases. Amylase and lipase are two very important enzymes that have been vastly studied and have great importance in different industries and therapeutic industry. In this review, an approach has been made to highlight the importance of different enzymes with special emphasis on amylase and lipase in the different industrial and medical fields.

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A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and Beyond

This review paper provides an overview regarding the main aspects of microbial lipases production. The most important microbial lipase-producing strains for submerged and solid-state fermentations are reviewed as well as the main substrates, including the use of agroindustrial residues. Current process techniques (batch, repeated-batch, fed-batch, and continuous mode) are discussed and the main bioreactors configurations are also presented. Furthermore, the present review paper shows a general overview about the development of mathematical models applied to lipase production. Finally, some future perspectives on lipase production are discussed with special emphasis on lipase engineering and the use of mathematical models as a useful tool for process improvement and control.

A Review on Microbial Lipases Production

Lipases (triacylglycerolacyl hydrolases, EC3.1.1.3) are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. In this review paper, an overview regarding the fungal lipase production, purification, and application is discussed. The review describes various industrial applications of lipase in pulp and paper, food, detergent, and textile industries. Some important lipase-producing fungal genera include Aspergillus, Penicillium, Rhizopus, Candida, etc. Current fermentation process techniques such as batch, fed-batch, and continuous mode of lipase production in submerged and solid-state fermentations are discussed in details. The purification of lipase by hydrophobic interaction chromatography is also discussed. The development of mathematical models applied to lipase production is discussed with special emphasis on lipase engineering.

Overview of fungal lipase: a review.

The production of extracellular enzymes by the thermophilic fungus Thermomyces lanuginosus was studied in chemostat cultures at a dilution rate of 0.08 h−1 in relation to variation in the ammonium concentration in the feed medium. Under steady state conditions, three growth regimes were recognised and the production of several extracellular enzymes from T. lanuginosus was recorded under different nutrient limitations ranging from nitrogen limitation to carbon/energy limitation. The range and the production of carbohydrate hydrolysing enzymes and lipase increased from Regime I (NH4Cl ≤ 600 mg l−1) to Regime III (NH4CI ≥ 1200 mg l−1), whereas production of protease was highest in Regime II (600 mg l−1 < NH4Cl <1200 mg l−1).

Enzyme production in continuous cultivation by the thermophilic fungus, Thermomyces lanuginosus

Effect of pH and the initial concentration of yeast extract on regulation of dimorphism and exopolysaccharide formation of Aureobasidium pullulans in batch culture

The ability of the yeast form of Aureobasidium pullullans to elaborate exopolysaccharide in chemostat culture at various pH values.

The yeast-mycelial dimorphic fungus Aureobasidium pullulans was grown in chemostat culture in mineral medium under zinc-limiting and zinc-sufficient conditions. The Zn2+ uptake of both the yeast and mycelial growth form conformed to saturation kinetics and the Zn2+ uptake appeared to be energy dependent and no efflux was demonstrated. No significant difference between the Km and Vmax values of the yeast and mycelial growth forms were found when grown under glucose-limiting (adequate zinc) conditions, with 7.6 μM Zn2+ in the feed medium. Growth conditions (zinc limitation or adequate zinc) were shown to influence the Zn2+ uptake capabilities as yeast cells harvested from zinc-limited chemostat culture had a higher affinity (Km=0.13 μM) and a higher Vmax (1.67 nmol Zn2+ min−1 (mg dry wt.)−1) than yeast cells harvested from zinc adequate chemostat culture (Km=0.36 μM; Vmax=0.64 nmol Zn2+ min−1 (mg dry wt.)−1).

M. Reeslev

Papers

Enzyme production in continuous cultivation by the thermophilic fungus, Thermomyces lanuginosus

Effect of pH and the initial concentration of yeast extract on regulation of dimorphism and exopolysaccharide formation of Aureobasidium pullulans in batch culture

The ability of the yeast form of Aureobasidium pullullans to elaborate exopolysaccharide in chemostat culture at various pH values.

Uptake of Zn2+ by yeast and mycelial growth form of Aureobasidium pullulans grown in chemostat culture