Addition Of Detergent Research Articles

State of knowledge about biotechnological uses of digestive enzymes of marine fishery resources: A worldwide systematic review

The characterization of digestive enzymes presents in fish and their potential biotechnological uses is a well-developed and studied field. However, there has not been a systematic review that analyzes the state of knowledge of these enzymes at a global level. Therefore, a systematic literature search on three platforms was carried out to review and analyze existing knowledge about digestive enzymes of marine fishes from fisheries and aquaculture and their potential application in industrial processes. Using the PRISMA method for selecting journal manuscripts, we found 112 scientific articles published between 1984 and 2020 studying different digestive enzymes from 87 fish species. Most studies were carried out in Tunisia and Mexico and only 6 articles were published in South American countries. The most studied digestive enzymes were alkaline proteases, mainly trypsin, and the proposed uses for these enzymes were mainly as additives in commercial detergents. There is a vacancy in the characterization of other digestive enzymes as pepsins, lipases and amylases and the study of species that are distributed in the Southwest Atlantic Ocean. It is necessary to expand the knowledge about other digestive enzymes and to carry out new studies in regions with an important fishery development.

Introducing Intermolecular Interaction to Strengthen the Stability of MnSOD Dimer.

Manganese superoxide dismutase from Staphylococcus equorum (MnSODSeq) maintains its activity upon treatments like a wide range of pH, addition of detergent and denaturing agent, exposure to ultraviolet light, and heating up to 50°C. The enzyme dimer dissociates at 52-55°C, while its monomer unfolds at 63-67°C. MnSOD dimeric form is indispensable for the enzyme activity; therefore, strengthening the interactions between the monomers is the most preferred strategy to improve the enzyme stability. However, to date, modification of MnSODSeq at the dimer interface has been unfruitful despite excluding the inner and outer sphere regions that are important to the enzyme activity. Here, a new strategy was developed and K38R-A121E/Y double substitutions were proposed. These mutants displayed similar enzyme activity to the wild type. K38R-A121E dimer was thermally more stable and its monomer stability was similar to the wild type. The thermal stability of K38R-A121Y dimer was similar to the wild type but its monomer was thermally less stable. In addition, the structure of the previously reported L169W mutant was also elucidated. The L169W mutant structure showed that intramolecular modification can decrease flexibility of the MnSODSeq monomer and leads to a less stable enzyme with similar activity to the wild type. Thus, while the enzyme activity depends on arrangement of residues in the dimer interface, the stability appears to depend more on its monomeric architecture. Furthermore, in the L169W structure in complex with azide, which is a specific inhibitor for MnSOD, one of the azide molecules was present in the dimer interface region that previously has been identified to involve in the enzymatic reaction. Nevertheless, the present results show that an MnSODSeq mutant with better thermal stability has been obtained.

Influenza virus and pneumococcal neuraminidases enhance catalysis by similar yet distinct sialic acid–binding strategies

Influenza A viruses and the bacterium Streptococcus pneumoniae (pneumococci) both express neuraminidases that catalyze release of sialic acid residues from oligosaccharides and glycoproteins. Although these respiratory pathogen neuraminidases function in a similar environment, it remains unclear if these enzymes use similar mechanisms for sialic acid cleavage. Here, we compared the enzymatic properties of neuraminidases from two influenza A subtypes (N1 and N2) and the pneumococcal strain TIGR4 (NanA, NanB, and NanC). Insect cell-produced N1 and N2 tetramers exhibited calcium-dependent activities and stabilities that varied with pH. In contrast, E.coli-produced NanA, NanB, and NanC were isolated as calcium insensitive monomers with stabilities that were more resistant to pH changes. Using a synthetic substrate (MUNANA), all neuraminidases showed similar pH optimums (pH 6-7) that were primarily defined by changes in catalytic rate rather than substrate binding affinity. Upon using a multivalent substrate (fetuin sialoglycans), much higher specific activities were observed for pneumococcal neuraminidases that contain an additional lectin domain. In virions, N1 and especially N2 also showed enhanced specific activity toward fetuin that was lost upon the addition of detergent, indicating the sialic acid-binding capacity of neighboring hemagglutinin molecules likely contributes to catalysis of natural multivalent substrates. These results demonstrate that influenza and pneumococcal neuraminidases have evolved similar yet distinct strategies to optimize their catalytic activity.

Оценка эффективности опытного пакета присадок к моторным маслам для современных бензиновых двигателей

A comparative evaluation of the experimental and imported additive packages in the composition of API SL/CF engine oil was carried out. It was found that the experimental package of PH-SL additives in the composition of engine oil has a stable colloidal structure, surpasses the imported package in terms of thermal oxidative stability and tendency to varnish formation and is on par with it in terms of tribological characteristics. During the monitoring of qualitative changes in the state of oxidized oils, including using the method of IR-Fourier spectrometry, it was found that oil with an experimental additive package has an advantage in changing the kinematic viscosity of oxidized oil and the degree of activation of detergent additives compared with oil containing an imported additive package. Based on the results of comparative tests on colloidal and operational properties, it was found that the experimental additive package is at the level of an imported analog. The effectiveness of the use of an experimental additive package instead of imported in the compositions of API SL/CF engine oils has been confirmed.

Quantitation of polyetheramines as the active components of detergent additives in gasoline by the ninhydrin reaction

The detergent additives added into gasoline can effectively reduce the accumulation of coke deposits in engine and improve the exhaust emission pollution. The cleaning effect of detergent additives depends on the contents and compositions of the active components which usually contain a terminal amino group. In this work, a quantitative method was established to determine the polyetheramines of detergent additives in gasoline by the ninhydrin reaction. Unlike the small molecule compounds containing amino groups, such as amino acids and alkylamines, the formation of vesicles significantly increased the reactivity between polyetheramines and ninhydrin. The ninhydrin reaction was prohibited when the vesicles of polyetheramines were destroyed by adding ethanol, which was confirmed by the mass spectrometry and dynamic light scattering results. At the optimized condition, the reaction between the polyetheramines and ninhydrin generated a blue-purple dye (Ruhemann’s purple) with a strong absorption at 560 nm. This reaction was highly selective, sensitive, and rapid. This quantitative method could distinguish the active components (polyetheramines) from the carrier oils (polyethers) in detergent additives. Aniline compounds in gasoline also did not interfere with the measurement of polyetheramines. The quantitative range was between 50 and 1000 mg/kg. The whole procedure could be finished in about 30 min. The accuracy of this method was verified using four different commercial polyetheramines and the results showed that the method was applicable to different types of detergent additives with relative errors lower than 10 %.

Optimization of detergents in solubilization and reconstitution of Aquaporin Z: A structural approach

BackgroundThe exceptional capacities of aquaporins in terms of water permeation and selectivity have made them an interesting system for membrane applications. Despite the multiple attempts for immobilizing the aquaporins over a porous substrate, there is a lack of studies related to the purification and reconstitution steps, principally associated with the use of detergents in solubilization and destabilization steps. This study analyzed the effect of detergents in Aquaporin Z solubilization, considering the purity and structural homogeneity of the protein. MethodsThe extraction process was optimized by the addition of detergent at the sonication step, which enabled the omission of the ultracentrifugation and resuspension steps. Two detergents, Triton X-100, and octyl-glucoside were also evaluated. Destabilization mediated by detergents was used as reconstitution method. Saturation and solubilization points were defined by detergent concentration and both, liposomes and proteoliposomes, were analyzed by size distribution and permeability assays. Detergent removal with Bio-beads was also analyzed. ResultsOctyl glucoside ensures structural stability and homogeneity of Aquaporin Z. However, high concentrations of detergents induce the presence of defects in proteoliposomes. While saturated liposomes create homogeneous and functional structures, solubilized liposomes get affected by a reassembly process, creating vesicle defects with anomalous permeability profiles. ConclusionsDetergent concentration affects the structural conformation of proteoliposomes in the reconstitution process. General significanceSince the destabilization process is dependent on vesicle, detergent, and buffer composition, optimization of this process should be mandatory for further studies. All these considerations will allow achieving the potential of Aquaporins and any other integral membrane protein in their applications for industrial purposes.

Simultaneous purification and characterization of detergent-stable, solvent-tolerant haloextremozymes protease and lipase from Haloferax sp. strain GUBF 2.

Industrial important proteases and lipases are in increasing demand for various biotechnological applications. In the present study, the concomitantly produced protease and lipase by Haloferax sp. strain GUBF 2 were simultaneously purified as a heterogeneous lipase (45 and 66kDa) and homogeneous protease (180kDa); with 28.3 and 31.36 fold purity, respectively using Sephadex G-200. The aforementioned extremozymes were active at pH 3-13, 20-80°C, 1-5M NaCl, with optimal activity at pH 6, 70°C, and 3M NaCl, thus exhibiting attributes of true haloextremozymes. The Km and Vmax of purified lipase were 3.47mM and 16.2U/mL, while protease were 3.29mg/mL and 28.5U/mL, respectively. FTIR bands corresponding to the vibrations of amide II and amide III were detected in haloextremozymes which could perhaps be used to determine the secondary structure of the purified proteins. Furthermore, the activity of both enzymes was stimulated by Ca2+ and inhibited by 10mM Hg2+ and phenylmethyl sulphonyl fluoride (PMSF). Additionally, these haloextremozymes are stable in the presence of detergent additives and organic solvents. In addition, purified protease displayed 74.3 ± 4.85% in-vitro blood clot dissolution activity. Conclusively this study revealed the key features, unusual properties, and possible biomedical applications of detergent-stable and organic solvent-tolerant haloextremozymes from Haloferax sp. strain GUBF 2 to date unexplored.

Characterization of Sphingobacterium sp. Ab3 Lipase and Its Coexpression with LEA Peptides.

Sphingobacterium sp. is a yellowish Gram-negative bacterium that is usually characterized by high concentrations of sphingophospholipids as lipid components. As microbial enzymes have been in high demand in industrial fields in the past few decades, this study hopes to provide significant information on lipase activities of Sphingobacterium sp., since limited studies have been conducted on the Sphingobacterium sp. lipase. A microbe from one collected Artic soil sample, ARC4, was identified as psychrotolerant Sphingobacterium sp., and it could grow in temperatures ranging from 0°C to 24°C. The expression of Sphingobacterium sp. lipase was successfully performed through an efficient approach of utilizing mutated group 3 late embryogenesis abundant (G3LEA) proteins developed from Polypedilum vanderplanki. Purified enzyme was characterized using a few parameters, such as temperature, pH, metal ion cofactors, organic solvents, and detergents. The expressed enzyme is reported to be cold adapted and has the capability to work efficiently under neutral pH (pH 5.0 to 7.0), cofactors like Na+ ion, and the water-like solvent methanol. Addition of nonionic detergents greatly enhanced the activity of purified enzyme. IMPORTANCE The mechanism of action of LEA proteins has remained unknown to many; in this study we reveal their presence and improved protein expression due to the molecular shielding effect reported by others. This paper should be regarded as a useful example of using such proteins to influence an existing expression system to produce difficult-to-express proteins.

Ultrastructure and stability of cellular nanoparticles isolated from Phaeodactylum tricornutum and Dunaliella tertiolecta conditioned media

Background: Cells in general secrete nanoparticles (NPs) which are believed to mediate intercellular communication. Recently, great efforts have been made to utilize them as delivery vectors. We aimed to harvest and identify NPs from liquid cultures of two marine microalgae Dunaliella tertiolecta and Phaeodactyum tricornutum. Methods: NPs were isolated from the culture conditioned media by differential ultracentrifugation by the protocol used for the isolation of extracellular vesicles. Microalgae and isolated NPs were examined by scanning electron microscopy (SEM) while isolated NPs were examined also by cryogenic transmission electron microscopy (cryo-TEM). The Triton X-100 detergent and temperature sensitivity of NPs was assessed by dynamic light scattering (DLS) through monitoring the intensity of the scattered light (I) and the distribution of hydrodynamic radii of NPs (Rh). Results: Two mechanisms of formation of NPs with average Rh 200 nm were observed in the D. tertiolecta culture: a disintegration of tubular protrusions, and cell decay. A part of the imaged D. tertiolecta NPs were membrane-enclosed vesicles, but the isolates also contained electron-dense NPs and nanofilaments. P. tricornutum NPs in the culture and in the isolate were homogeneous in size and shape. Their average Rh was 104 nm. The addition of surfactant to isolates resulted in a change in Rh distribution and a decrease of I in samples from both species, indicating decay of a part of NPs. Changes in the width of the I(Rh) peaks were observed at temperatures above 45 °C. Conclusions: A part of NPs found in isolates from microalgae D. tertiolecta and P. tricornutum were membrane-enclosed vesicles. However, the isolates obtained by a standard protocol for extracellular vesicle isolation by ultracentrifugation contained also a significant amount of other similar-sized nanoparticles. The isolates were partly susceptible to the addition of detergent and to temperature up to 80 degrees.

Is Gigartina a potential source of food protein and functional peptide-based ingredients? Evaluating an industrial, pilot-scale extract by proteomics and bioinformatics

Seaweeds attract substantial interest as novel sources of sustainable food protein, as they are established sources of industrial hydrocolloids with reasonable protein content. In this study, we investigate the protein composition and nutritional quality of a seaweed protein extract (SPE) from Gigartina sp. The SPE displayed low (<2%), but pH-dependent, aqueous solubility likely due to the harsh conditions employed during extraction. Solubility improved using alkaline buffering and detergent addition to facilitate proteomic characterization by quantitative LC-MS/MS. Proteomics analysis revealed that SPE was dominated by proteins related to light harvest and particularly phycobiliproteins (44%), where phycoerythrin was most abundant (28%). Based on subcellular localization, the extraction method was evaluated as good for release of cellular protein. SPE was rich in essential amino acids (36–41%) and particularly branched chain amino acids (22–24%), and thereby a potential source of nutritional food protein. Using bioinformatic prediction and structural modelling, we found abundant SPE proteins contained novel peptides with the amphiphilic properties required to stabilize an oil/water interface, and thereby high probability of being potent emulsifiers. Based on this study, Gigartina sp. could serve a good candidate for extraction of sustainable, nutritious food protein, with the possibility of further processing into hydrolysates with strong emulsifying properties for use as natural food ingredients.

Green synthesis and antimicrobial mechanism of nanoparticles: applications in agricultural and agrifood safety.

The growing demand for food and its safety are a challenge for agriculture and agrifood. This has led to the incorporation of alternatives such as organic agriculture, the use of biocontrollers, the development of transgenic plants resistant to pathogens and the incorporation of nanotechnology. In this sense, agrochemicals based on nanoparticles (NPs) have been developed. Recently, the green synthesis of NPs has grown rapidly and, for this reason, molecules, microorganisms, fungi and plants are used. Synthesis from plant extracts offers a broad spectrum and, despite the fact that NPs are usually dispersed in size and shape, extensive antimicrobial effectiveness has been demonstrated at nanomolar concentrations. It has been shown that the mechanism of action can be through the dissipation of the driving force of the protons, the alteration of cellular permeability, the formation of bonds with the thiol group of the proteins, the generation of reactive species of oxygen, and the hyperoxidation of DNA, RNA and even the cell membrane. To improve the efficiency of NPs, modifications have been made such as coating with other metals, the addition of antibiotics, detergents and surfactants, as well as the acidification of the solution. Consequently, NPs are considered as a promising method for achieving safety in the agricultural and agrifood area. However, it is necessary to investigate the side effects of NPs, when applied in agroecological systems, on the textural, nutriment and sensory properties of food, as well as the impact on human health. © 2022 Society of Chemical Industry.

A Unique Enhancement of Propionibacterium freudenreichii's Ability to Remove Pb(II) from Aqueous Solution by Tween 80 Treatment.

Microbial agents have promise for the bioremediation of Pb(II)-polluted environments and wastewater, the biodecontamination of foods, and the alleviation of toxicity in living organisms. The dairy bacterium Propionibacterium freudenreichii is poorly able to remove Pb(II) from aqueous solution at 25 ppm, ranging from 0 to 10% of initial concentration. Here, we report on an original strong enhancement of this activity (ranging from 75% to 93%, p < 0.01) following the addition of a polysorbate detergent (Tween® 80) during or either shortly after the growth of a P. freudenreichii culture. We evaluated the optimal Tween® 80 concentration for pretreatment conditions, documented the role of other detergents, and explored the possible mechanisms involved. Our results reveal a novel, environmentally friendly, low-cost pretreatment procedure for enhancing the selective removal of lead from water by probiotic-documented bacteria.

PvdM of fluorescent pseudomonads is required for the oxidation of ferribactin by PvdP in periplasmic pyoverdine maturation

Fluorescent pseudomonads such as Pseudomonas aeruginosa or Pseudomonas fluorescens produce pyoverdine siderophores that ensure iron-supply in iron-limited environments. After its synthesis in the cytoplasm, the nonfluorescent pyoverdine precursor ferribactin is exported into the periplasm, where the enzymes PvdQ, PvdP, PvdO, PvdN, and PtaA are responsible for fluorophore maturation and tailoring steps. While the roles of all these enzymes are clear, little is known about the role of PvdM, a human renal dipeptidase–related protein that is predicted to be periplasmic and that is essential for pyoverdine biogenesis. Here, we reveal the subcellular localization and functional role of PvdM. Using the model organism P. fluorescens, we show that PvdM is anchored to the periplasmic side of the cytoplasmic membrane, where it is indispensable for the activity of the tyrosinase PvdP. While PvdM does not share the metallopeptidase function of renal dipeptidase, it still has the corresponding peptide-binding site. The substrate of PvdP, deacylated ferribactin, is secreted by a ΔpvdM mutant strain, indicating that PvdM prevents loss of this periplasmic biosynthesis intermediate into the medium by ensuring the efficient transfer of ferribactin to PvdP in vivo. We propose that PvdM belongs to a new dipeptidase-related protein subfamily with inactivated Zn2+ coordination sites, members of which are usually genetically linked to TonB-dependent uptake systems and often associated with periplasmic FAD-dependent oxidoreductases related to d-amino acid oxidases. We suggest that these proteins are necessary for selective binding, exposure, or transfer of specific d- and l-amino acid–containing peptides and other periplasmic biomolecules in manifold pathways.

Characterization and Purification of Alkaline Protease from Novel Bacillus subtilus MS1 for Detergent Additives

Characterization and Purification of Alkaline Protease from Novel Bacillus subtilus MS1 for Detergent Additives

Giα and β Proteins Associate in a Complex with Cannabinoid Receptor Interacting Protein 1a (CRIP1a)

Cannabis usage in recent years has increased due to the legalization of both recreational and medical use. The CB1cannabinoid receptor (CB1R) is a G‐protein coupled receptor (GPCR) found in the central nervous system and modulates neuroprogenitor development, neural commitment and migration, and neurotransmitter release. Cannabinoid receptor interacting protein 1a (CRIP1a) is a beta‐barrel protein that interacts with CB1R. Fluorescence polarization studies demonstrated that CRIP1a interacts directly with myristoylated Gαi (Booth et. al. 2021). We hypothesized that this occurs through the intercalation of the myristoyl moiety into the interior of the barrel through a gapped site that is bordered by the C‐terminal β‐strand. We tested this hypothesis by immunoprecipitation of CRIP1a with antibodies developed to two different epitopes of CRIP1a: to the loop‐helix‐loop motif that is located at a distance from the proposed myristoylated peptide access site, and to the C‐terminal β‐strand of CRIP1a which is directly adjacent to this region. We immunoprecipitated CRIP1a from N18TG2 mouse neuroblastoma cell homogenates without the addition of detergent for solubilization. We then probed for CRIP1a and determined if the either the Gαi subunit or the Gβγ dimer were associated with CRIP1a. Immunoprecipitation using the antibody to CRIP1a directed at the loop‐helix‐loop motif revealed complexes with Gai1 and Gai3 and not Gβγ. In contrast, immunoprecipitation of CRIP1a using the antibody directed at the C‐terminal β‐strand co‐immunoprecipitated Gβ and not Gαi1 or Gαi3. Collectively, these data suggest CRIP1a is a cargo‐carrying protein capable of carrying the G‐protein α‐subunit, but also exhibits an interaction with the β‐subunit.

Effect of detergents on froth stability and flotation separation

Abstract Froth stability is an important factor in determining flotation yield, and one of the factors affecting froth stability is dependent on the concentration and type of surfactant. Since detergents contain different types of surfactants, it is possible that they affect the froth stability (together with the frothing agent and the collector) and consequently the flotation yield. Therefore, the effect of detergents containing lauryldimethylamine oxide and sodium laureth sulphate was investigated in this study. The results showed that the addition of detergents increased the froth stability by more than 30% and 45% in terms of froth formation and froth decay, respectively. The flotation tests also showed that the addition of detergents increased the sulphur content of the concentrate by about 0.7%.

Impact of diesel and detergent contamination on gasoline low-speed pre-ignition and their characterization using unwashed gums

Fuel composition variability affects many aspects of engine operation. This includes the propensity to trigger abnormal combustions. Fuel logistic can lead to incorporating different contaminants into gasoline. Diesel fuel or over-concentrated detergent additives are two examples. They require a qualification and quantification within the gasoline fuel and an evaluation of their impact on engine performances.We consider both contaminants in this work and it addresses simultaneously their identification within a gasoline fuel and their impact on abnormal combustion. The study evaluates contaminants propensity to trigger Low Speed Pre-Ignition (LSPI). The latter is a stochastic abnormal combustion leading to engine damage related to fuel quality. A novel method based on unwashed gums is used to characterize qualitatively and quantitatively these contaminants. Engine tests led to the conclusion that diesel contamination contributes to increase LSPI frequency and severity. However, this increase depends on the base fuel heavy aromatic content. Deposit control additive (DCA) increases slightly LSPI frequency compared to diesel contaminant. The study also suggests that such additive can contribute to recover a less sensitive combustion system once it has been running with a diesel contaminated gasoline. Finally, this work explores the possibility of correlating fuel propensity to trigger LSPI through unwashed gums (UWG) measurement. It concludes that the approach seems sensible but requires further work to be confirmed.

Interaction of human erythrocyte catalase with air-water interface in cryoEM.

One of the key goals in single-particle cryo-microscopy is to obtain a uniform distribution of particle orientations, so that the three-dimensional structure has isotropic resolution in Fourier space. A common problem arises from the interaction of protein molecules with the air–water interface that exists on both surfaces of the thin film of liquid that is formed prior to plunge-freezing into liquid ethane. Some proteins and other macromolecular complexes are disrupted by interaction with the air–water interface. Other proteins or macromolecules either become concentrated through their interaction with the interface or are excluded because they bind strongly to some other part of the grid or the filter paper used in blotting. In this paper, the interaction of human erythrocyte catalase with the air–water interface is investigated and minimized by the addition of certain detergents. Detergents can form an amphipathic monolayer at the air–water interface that creates a barrier and leaves the molecules free to adopt a variety of orientations, thus facilitating the 3D structure determination. These results suggest that further characterization and development of detergents for cryo-microscopy plunge-freezing would be useful.

Optimal Irrigant in High Pressure Paint Injection Injuries of the Hand.

Background:High pressure injection injury to the hand with paint leads to amputation rates near 48%. Historically, authors utilized saline irrigation alone, but have high reoperation rates. We conducted a cadaveric study to determine the ideal detergent for effective paint removal from the soft tissue.Methods:Two cadaveric hands were amputated from the same cadaver. The left and right hand digits were injected with flat white latex-based paint and flat white oil-based paint, respectively. Each digit received a longitudinal incision and was scrubbed for 120 seconds with 50 mL of a randomly assigned detergent and no detergent (saline) as the control. After achieving a lather, each finger was cleansed with 50 mL saline before being evaluated by two blinded hand surgery faculty. Reviewers assessed the washouts as adequate or inadequate, in order to generate a Kappa statistic and measure inter-rater reliability prior to ranking each digit (1 through 5) (ie, 1 = most paint-free soft tissue).Results:The two hand faculty had an inter-rater reliability of 0.70. Both reviewers ranked povidone-iodine 10% or Johnson & Johnson shampoo as the best irrigant for latex-based paint. In oil-based paint, povidone-iodine 10%, Johnson & Johnson, & Techni-care were ranked as top three. All reviewers reported detergents were better than saline alone.Conclusions:The addition of detergent created an irrigant that removed both latex- and oil-based paint better than normal saline alone. Based on these results, surgeons treating high-pressure injection injury should consider using Povidone-Iodine 10% or Johnson & Johnson baby shampoo for latex- or oil-based paint.

Reduction of Promiscuous Peptides-Enzyme Inhibition and Aggregation by Negatively Charged Biopolymers.

In this work, peptides selected from a microarray were found to inhibit β-gal with promiscuous mechanisms. Peptides inhibited the enzyme in a noncompetitive kinetics, and the inhibition of enzyme activities was reduced under high enzyme concentrations and the addition of detergent. Dynamic light scattering and atomic force microscope revealed that peptide/enzyme aggregation was related to inhibited enzyme activities. Positively charged residues of arginine and lysine were critical for the enzyme inhibition. The preincubation of peptide inhibitors with negatively charged biopolymers of polyphosphates, ssDNA, and low pI peptides could increase the residual activity of peptide-inhibited enzyme, possibly due to the disruption of the electrostatic interaction between positively charged peptide residues and the β-gal surface. Further, negative biopolymers were able to recover the activity of the aggregated peptide/β-gal complex. Negatively charged biopolymers could be used in high-throughput screening assays to reduce peptides/protein aggregation and thereby minimize promiscuous inhibitions.