A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values

Morellon‐Sterling, Roberto; Tavano, Olga Luisa; Bolívar, Juan M.; Berenguer-Murcia, Ángel; Vela‐Gutiérrez, Gilber; Sabir, Jamal S.M.; Tacias-Pascacio, Veymar G.; Fernández‐Lafuente, Roberto

doi:10.1016/j.ijbiomac.2022.04.224

Cited by 46 publications

(26 citation statements)

References 318 publications

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“…Optimum pH (pH at which enzyme activity is maximum) and pH stability (pH range at which enzyme is active) have essential effects on pepsin enzyme activity, so enzyme activity decreases when pH is out of its optimal value [35]. Since pepsin is a type of acidic protease, its activity is maintained at low pH values, and Its activity has been attributed to protein denaturation at a pH above 6 [20,35,37]. Generally, if the studied sh has more than one type of pepsin, their optimal pH is usually similar, but this may not be the case for all species [37].…”

Section: Optimum Ph and Ph Stabilitymentioning

confidence: 99%

“…Temperatures lower or higher than the optimal temperature decrease the activity of sh pepsin. Further, pepsin obtained from sh has a highly variable optimal temperature based on the species of sh used [35,36]. Also, the optimal temperature for cold-water shes is lower than for warm-water shes.…”

Section: Biochemical Characterization Of Pepsin Puri Ed S Commerson V...mentioning

confidence: 99%

“…Pepsin from different types of sh has different optimal temperatures, and pepsin extracted from cold-water shes tends to have lower optimal temperatures than those from warm-water shes [37,38]. It is clear that the pepsin enzymes obtained from cold-water shes have a lower activation energy for Arenos formation, which explains their lower optimum temperature and higher stability temperature compared to those obtained from warmwater shes [35,37]. Nalinanon et al [34] reported that pepsin obtained from albacore tuna had a temperature stability range of 20 °C to 50 °C while increasing the temperature above 50 °C led to a signi cant decrease in stability.…”

Section: Biochemical Characterization Of Pepsin Puri Ed S Commerson V...mentioning

confidence: 99%

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Purification and characterization of pepsin enzyme from Scomberomorus commerson mackerel’s stomach by aluminum hydroxide, and improved its thermal stability by graphene oxide nanosheet

Shobar

Rezaei

Naghdi

et al. 2023

Preprint

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In the present study, pepsinogen enzyme was purified from the S. commerson viscera in 7 steps, including; (1) using a buffer containing NaCl and CaCl2, (2) Acidification, (3) precipitation by dried sulfate ammonium, (4) Aluminum hydroxide gel, (5) Saturated ammonium sulfate, (6) Gel filtration Sephadex G-50, and (7) Anion-exchange DEAE-cellulose. Purified pepsinogen converted into pepsin quickly at pH 2.0, and its optimum pH and temperature were 2, and 37 °C. Hence, ammonium sulfate with 67/5 % saturation showed the highest activity and protein precipitation. Besides, results showed that 18% Alum gel had the highest enzyme activity in the precipitate formed during dialysis. Furthermore, pepsin activity was stopped above 50 °C, but immobilized pepsin on GO-PEG maintained it up to a temperature of 65 °C. Purified pepsin was completely inactive in the presence of 0.1 M pepstatin A. Catalytic constants KM and kcat for proteolysis of acid-denatured hemoglobin were 35/39 ± 0.03 M, and 5.3 ± 0.002 × 10 -5 S-1, respectively. Finally, based on the obtained results, it can be suggested that the use of aluminum hydroxide gel and graphene oxide can be a suitable approach for purifying pepsin enzyme from fish viscera and improving their thermal stability.

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Section: Optimum Ph and Ph Stabilitymentioning

confidence: 99%

Section: Biochemical Characterization Of Pepsin Puri Ed S Commerson V...mentioning

confidence: 99%

Section: Biochemical Characterization Of Pepsin Puri Ed S Commerson V...mentioning

confidence: 99%

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Purification and characterization of pepsin enzyme from Scomberomorus commerson mackerel’s stomach by aluminum hydroxide, and improved its thermal stability by graphene oxide nanosheet

Shobar

Rezaei

Naghdi

et al. 2023

Preprint

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“…Extensive research was performed by Fernandez-Lafuente et al regarding stabilization of enzymes via immobilization [ 13 , 14 , 15 , 16 , 17 , 18 , 19 ]. Enzyme immobilization must be designed not only to solve the problem of enzyme recovery and reusability, but also to improve enzymes features, such as stability, activity, specificity, and selectivity.…”

Section: Introductionmentioning

confidence: 99%

(Magnetic) Cross-Linked Enzyme Aggregates of Cellulase from T. reesei: A Stable and Efficient Biocatalyst

et al. 2023

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Cross-linked enzyme aggregates (CLEAs) represent an effective tool for carrier-free immobilization of enzymes. The present study promotes a successful application of functionalized magnetic nanoparticles (MNPs) for stabilization of cellulase CLEAs. Catalytically active CLEAs and magnetic cross-linked enzyme aggregates (mCLEAs) of cellulase from Trichoderma reesei were prepared using glutaraldehyde (GA) as a cross-linking agent and the catalytic activity and stability of the CLEAs/mCLEAs were investigated. The influence of precipitation agents, cross-linker concentration, concentration of enzyme, addition of bovine serum albumin (BSA), and addition of sodium cyanoborohydride (NaBH3CN) on expressed activity and immobilization yield of CLEAs/mCLEAs was studied. Particularly, reducing the unsaturated Schiff’s base to form irreversible linkages is important and improved the activity of CLEAs (86%) and mCLEAs (91%). For increased applicability of CLEAs/mCLEAs, we enhanced the activity and stability at mild biochemical process conditions. The reusability after 10 cycles of both CLEAs and mCLEAs was investigated, which retained 72% and 65% of the initial activity, respectively. The thermal stability of CLEAs and mCLEAs in comparison with the non-immobilized enzyme was obtained at 30 °C (145.65% and 188.7%, respectively) and 50 °C (185.1% and 141.4%, respectively). Kinetic parameters were determined for CLEAs and mCLEAs, and the KM constant was found at 0.055 ± 0.0102 mM and 0.037 ± 0.0012 mM, respectively. The maximum velocity rate (Vmax) was calculated as 1.12 ± 0.0012 µmol/min for CLEA and 1.17 ± 0.0023 µmol/min for mCLEA. Structural characterization was studied using XRD, SEM, and FT-IR. Catalytical properties of immobilized enzyme were improved with the addition of reducent NaBH3CN by enhancing the activity of CLEAs and with addition of functionalized aminosilane MNPs by enhancing the activity of mCLEAs.

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“…Moreover, enzymes located in pore channels are protected against microbial attack and physical/mechanical damage. 29 …”

Section: Introductionmentioning

confidence: 99%

Preparation of immobilized pepsin for extraction of collagen from bovine hide

Duan

Cheng

2022

RSC Adv.

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A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values

Cited by 46 publications

References 318 publications

Purification and characterization of pepsin enzyme from Scomberomorus commerson mackerel’s stomach by aluminum hydroxide, and improved its thermal stability by graphene oxide nanosheet

Purification and characterization of pepsin enzyme from Scomberomorus commerson mackerel’s stomach by aluminum hydroxide, and improved its thermal stability by graphene oxide nanosheet

(Magnetic) Cross-Linked Enzyme Aggregates of Cellulase from T. reesei: A Stable and Efficient Biocatalyst

Preparation of immobilized pepsin for extraction of collagen from bovine hide

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