Enzyme Activity Measurement for Phospholipase A1

Creative Enzymes is committed to being the most reliable service provider in the field of enzyme assays. We are well known for the high rate of customer satisfaction. Our prompt service, best customer care, and dedicated resources have made us a most preferred vendor in the global market. Herein, Creative Enzymes is proud to offer the precise enzymatic assay for phospholipase A1.

Phospholipase A1 (EC 3.1.1.32; phosphatidylcholine 1-acylhydrolase; PLA₁) is an enzyme that hydrolyzes ester bonds of phospholipids at the sn-1 position and yields 2-acyl-lysophospholipids and fatty acids (FFAs). Both phospholipase A1 and phospholipase A2 (EC 3.1.1.4; phosphatidylcholine 2-acylhydrolase; PLA₂) cleave glycerophospholipids into lysophospholipid and free fatty acids. They are classified as PLA₁ and PLA₂ based on whether they cleave the sn-1 or sn-2 position of phospholipids, respectively. PLA₁ activities have been detected in many cells and tissues from various organisms, such as rat platelets, bovine brain, testis, hornet venom, bonito muscle, and fungi. Recently, several PLA₁ isozymes have been identified and much has been learned about the structure and molecular function of PLA₁. Currently nine PLA1 enzymes are known in mammals; six are extracellular enzymes and the other three are intracellular enzymes. The intracellular and extracellular PLA₁’s share no sequence homologies and apparently have distinct functions. Some PLA₁’s have a broad substrate specificity and hydrolyze both phospholipids and triacylglycerol (TG) as well as galactolipids. By contrast, other PLA₁’s such as phosphatidylserine (PS)-specific PLA₁ (PS-PLA₁), membrane-associated phosphatidic acid (PA)-selective PLA₁α (mPA-PLA₁α), and mPA-PLA1β show a strict substrate specificity and specifically act on PS and PA. These PLA₁’s may play a specific role in yielding bioactive lysophospholipids, lysophosphatidylserine (LPS), and lysophosphatidic acid (LPA). All extracellular PLA₁ molecules belong to the pancreatic lipase gene family.

Figure 1: Catalytic reactions and products of PLA₁ and PLA₂.
Reference: Murayama K, Kano K, Matsumoto Y, et al. Journal of structural biology, 2013, 182(2): 192-196.

Functionally, PLA₁’s play a pivotal role in medicine, nutrition, pharmaceutical, and food industries. For example, the recombinant PLA₁ represents a good candidate for wasp venom immunotherapy. Moreover, PLA₁ improves the foaming stability and properties of skim milk and whey, implying that PLA₁ can be a useful tool for modifying the functionality of dairy products and ingredients. Recently, PLA₁ has been reported as a potential processing aid in cheese-making, and a significant increase of cheese yield on a pilot as well as on an industrial scale was reported. Ultimately, it can be seen that PLA₁’s serve as a critical part in many processes, and thus more detailed studies on these enzymes will start soon, which rely on proper enzymatic assays.

Creative Enzymes is a leading company of high-quality bioanalytical services and contract custom research specialized in enzyme activity analysis serving the needs of clients from the pharmaceutical, biotechnological, and environmental industries. We are fully prepared to offer the accurate activity assays for PLA₁’s. The activities of PLA₁’s are determined by using the fluorometric assays. Our test results are the most trusted and proven in the global market. Overall, Creative Enzymes is your best choice during development of products containing PLA₁.

Figure 2: Ribbon representation of the PLA₁ structure from Streptomyces albidoflavus NA297. Secondary structural elements are colored blue (helices) and pink (strands); aa residues in the active site are indicated as stick models.
Reference: Murayama K, Kano K, Matsumoto Y, et al. Journal of structural biology, 2013, 182(2): 192-196.