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A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 45446

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Special Issue Editors

Prof. Dr. Chia-Hung Kuo

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Guest Editor

Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung 81157, Taiwan
Interests: food analysis; food processing; cellulase; lipase esterification and trans esterification; amylase; enzymatic kinetics; ultrasound-assisted enzymatic reaction; enzyme extraction; biotransformation; sacchariﬁcation; response surface methodology; artificial neural network; wine fermentation
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Chwen-Jen Shieh

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Guest Editor

Biotechnology Center, National Chung-Hsing University, Taichung, Taiwan
Interests: biodiesel; lipid biocatalysis; enzyme technology; bioprocess optimization; supercritical fluid technology; Chinese herb medicine biotechnology
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Hui-Min David Wang

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Guest Editor

Graduate Institute of Biomedical Engineering, National Chung Hsing University, Taichung, Taiwan
Interests: tissue engineering; regenerative medicine; drug design; cancer research; food chemistry; dermatology; biochemistry; chemical engineering; proteomics; molecule biology; marine biotechnology & resources
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are proteins produced by living cells to catalyze reactions, so-called biocatalysts. Enzymes can be produced from animals, plants and microorganisms through extraction and separation. Enzymes have become increasingly popular and are frequently applied in industry because they are highly specific and high catalytic efficiencies. Enzymes offer several advantages in terms of improved reaction selectivity, reduced energy costs, enhanced reliability, environmental friendliness and sustainability. Enzymes are currently widely used in the food industry, pharmaceutical industry, cosmetic industry, and biomedical industry. Many enzymes are used for these applications, such as lipase, protease, amylase, transferases, oxidoreductases, lactase, sucrase, maltase, pectinase, glucosidase, xylanase, cellulase, coenzyme Q10, superoxide dismutase, and peroxidase enzymes. Enzymes are used in the food industry for applications such as starch liquefaction, bread quality improvement, the production of prebiotic food ingredients, flavor improvement, animal feed treatment, and clarification. Enzymes are also used in cosmetics to prevent acne, skin aging, and pigmentation. Increasingly, enzymes are being used in medical applications, including therapeutics, drug delivery, and diagnostics. Therefore, various studies on enzymes have been developed, including those investigating enzyme production, purification, enzyme kinetics, enzyme immobilization, enzyme reactors, biotransformation, the synthesis of bioactive chemical compounds, valuable produce products, as well as enzyme application in analysis, biomedicine and biosensors.

In this Special Issue, we welcome original research articles and reviews focused on all aspects of enzymes used for the food, pharmaceutical, cosmetic, and biomedical industries. Research can be related to biocatalysis, process optimization, ultrasonic processes, food production, fermentation, enzyme-assisted extraction, enzyme production, biocatalytic processes, bio-reactors, food processing, biomass utilization, bioresource application, bio-transformations, enzymology, biological activity, enzymatic synthesis of value-added compounds, nanotechnology, biomedical applications, cosmetic applications, bioremediation and so on.

Prof. Dr. Chia-Hung Kuo
Prof. Dr. Chwen-Jen Shieh
Prof. Dr. Hui-Min David Wang
Guest Editors

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Keywords

enzyme production
enzyme purification
biocatalysis
optimization
lipase
cellulase
protease
amylase
biofuels
enzymatic-catalyzed synthesis
enzyme immobilization
biomass utilization
environmental protection
glucosidase
biotransformation
enzymatic kinetics
ultrasound-assisted enzymatic reaction
bio-reactor
enzymatic-assisted extraction
experimental design
response surface methodology (RSM)
artiﬁcial neural network (ANN)
drug design
cancer research
food chemistry
dermatology
biochemistry
chemical engineering
proteomics
molecule biology
marine biotechnology & resources

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Published Papers (14 papers)

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Editorial

Jump to: Research, Review

5 pages, 181 KiB

Open AccessEditorial

Enzymes in Biomedical, Cosmetic and Food Application

by Chia-Hung Kuo, Hui-Min David Wang and Chwen-Jen Shieh

Catalysts 2024, 14(3), 162; https://doi.org/10.3390/catal14030162 - 22 Feb 2024

Viewed by 2977

Abstract

Enzymes play an important role in biomedical, cosmetic and food applications, and their effects are mainly related to their specific reactions and catalytic activity [...] Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

Research

Jump to: Editorial, Review

17 pages, 2326 KiB

Open AccessFeature PaperArticle

Comparative Evaluation of the Asymmetric Synthesis of (S)-Norlaudanosoline in a Two-Step Biocatalytic Reaction with Whole Escherichia coli Cells in Batch and Continuous Flow Catalysis

by Adson Hagen Arnold and Kathrin Castiglione

Catalysts 2023, 13(10), 1347; https://doi.org/10.3390/catal13101347 - 5 Oct 2023

Viewed by 1190

Abstract

Opioids are important analgesics, and their pharmaceutical application is increasing worldwide. Many opioids are based on benzylisoquinoline alkaloids (BIA) and are still industrially produced from Papaver somniferum (opium poppy). (S)-norlaudanosoline ((S)-NLS) is a complex BIA and an advanced intermediate for diverse pharmaceuticals. The efficient synthesis of this scaffold could pave the way for a plant-independent synthesis platform. Although a promising biocatalytic route to (S)-NLS using norcoclaurine synthase (NCS) and ω-transaminase (TAm) has already been explored, the cost-effectiveness of this process still needs much improvement. Therefore, we investigated whether the synthesis could also be performed using whole cells to avoid the use of (partially) purified enzymes. With an optimized mixing ratio of TAm- and NCS-containing cells in batch biotransformations, 50 mM substrate was converted within 3 h with more than 90% yield and a high enantiomeric excess of the product (95%). To further increase the space–time yield, the cells were immobilized to enable their retainment in fixed-bed reactors. A comparison of glass beads, Diaion HP-2MG and alginate revealed that the addition of Diaion during bacterial growth led to the most active immobilisates. To facilitate sustained production of (S)-NLS, a fixed-bed setup was constructed based on lithographically printed columns from biocompatible PRO-BLK 10 plastic. The continuous production at two scales (5 mL and 50 mL columns) revealed insufficient system stability originating from biocatalyst leaching and inactivation. Thus, while the use of whole cells in batch biotransformations represents an immediate process improvement, the transfer to flow catalysis needs further optimization. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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16 pages, 2400 KiB

Open AccessFeature PaperArticle

Thermodynamic and Kinetic Investigation on Aspergillus ficuum Tannase Immobilized in Calcium Alginate Beads and Magnetic Nanoparticles

by Jônatas de Carvalho-Silva, Milena Fernandes da Silva, Juliana Silva de Lima, Tatiana Souza Porto, Luiz Bezerra de Carvalho, Jr. and Attilio Converti

Catalysts 2023, 13(9), 1304; https://doi.org/10.3390/catal13091304 - 18 Sep 2023

Cited by 5 | Viewed by 1383

Abstract

Tannase from Aspergillus ficuum was immobilized by two different techniques for comparison of kinetic and thermodynamic parameters. Tannase was either entrapped in calcium alginate beads or covalently-immobilized onto magnetic diatomaceous earth nanoparticles. When immobilized on nanoparticles, tannase exhibited lower activation energy (15.1 kJ/mol) than when immobilized in alginate beads (31.3 kJ/mol). Surprisingly, the thermal treatment had a positive effect on tannase entrapped in alginate beads since the enzyme became more solvent exposed due to matrix leaching. Accordingly, the proposed mathematical model revealed a two-step inactivation process. In the former step the activity increased leading to activation energies of additional activity of 3.1 and 26.8 kJ/mol at 20–50 °C and 50–70 °C, respectively, while a slight decay occurred in the latter, resulting in the following thermodynamic parameters of denaturation: 14.3 kJ/mol activation energy as well as 5.6–9.7 kJ/mol standard Gibbs free energy, 15.6 kJ/mol standard enthalpy and 18.3–29.0 J/(K·mol) standard entropy variations. Conversely, tannase immobilized on nanoparticles displayed a typical linear decay trend with 43.8 kJ/mol activation energy, 99.2–103.1 kJ/mol Gibbs free energy, 41.1–41.3 kJ/mol enthalpy and −191.6/−191.0 J/(K·mol) entropy of denaturation. A 90-day shelf-life investigation revealed that tannase immobilized on nanoparticles was approximately twice more stable than the one immobilized in calcium alginate beads, which suggests its use and recycling in food industry clarification operations. To the best of our knowledge, this is the first comparative study on kinetic and thermodynamic parameters of a tannase produced by A. ficuum in its free and immobilized forms. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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12 pages, 2972 KiB

Open AccessFeature PaperEditor’s ChoiceArticle

Identification of Cytochrome P450 Enzymes Responsible for Oxidative Metabolism of Synthetic Cannabinoid (1-Hexyl-1H-Indol-3-yl)-1-naphthalenyl-methanone (JWH-019)

by Ngoc Tran, William E. Fantegrossi, Keith R. McCain, Xinwen Wang and Ryoichi Fujiwara

Catalysts 2023, 13(6), 1008; https://doi.org/10.3390/catal13061008 - 15 Jun 2023

Viewed by 1575

Abstract

(1-Hexyl-1H-indol-3-yl)-1-naphthalenyl-methanone (JWH-019) is one of the second-generation synthetic cannabinoids which as a group have been associated with severe adverse reactions in humans. Although metabolic activation can be involved in the mechanism of action, the metabolic pathway of JWH-019 has not been fully investigated. In the present study, we aimed to identify the enzymes involved in the metabolism of JWH-019. JWH-019 was incubated with human liver microsomes (HLMs) and recombinant cytochrome P450s (P450s or CYPs). An animal study was also conducted to determine the contribution of the metabolic reaction to the onset of action. Using an ultra-performance liquid chromatography system connected to a single-quadrupole mass detector, we identified 6-OH JWH-019 as the main oxidative metabolite in HLMs supplemented with NADPH. JWH-019 was extensively metabolized to 6-OH JWH-019 in HLMs with the K_M and V_max values of 31.5 µM and 432.0 pmol/min/mg. The relative activity factor method estimated that CYP1A2 is the primary contributor to the metabolic reaction in the human liver. The animal study revealed that JWH-019 had a slower onset of action compared to natural and other synthetic cannabinoids. CYP1A2 mediates the metabolic activation of JWH-019, contributing to the slower onset of its pharmacological action. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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11 pages, 2605 KiB

Open AccessArticle

Metagenomic Type IV Aminotransferases Active toward (R)-Methylbenzylamine

by Rokas Statkevičius, Justas Vaitekūnas, Rūta Stanislauskienė and Rolandas Meškys

Catalysts 2023, 13(3), 587; https://doi.org/10.3390/catal13030587 - 15 Mar 2023

Cited by 1 | Viewed by 1656

Abstract

Aminotransferases (ATs) are pyridoxal 5′-phosphate-dependent enzymes that catalyze the reversible transfer of an amino group from an amino donor to a keto substrate. ATs are promising biocatalysts that are replacing traditional chemical routes for the production of chiral amines. In this study, an in silico-screening of a metagenomic library isolated from the Curonian Lagoon identified 11 full-length fold type IV aminotransferases that were successfully expressed and used for substrate profiling. Three of them (AT-872, AT-1132, and AT-4421) were active toward (R)-methylbenzylamine. Purified proteins showed activity with L- and D-amino acids and various aromatic compounds such as (R)-1-aminotetraline. AT-872 and AT-1132 exhibited thermostability and retained about 55% and 80% of their activities, respectively, even after 24 h of incubation at 50 °C. Active site modeling revealed that AT-872 and AT-4421 have an unusual active site environment similar to the AT of Haliscomenobacter hydrossis, while AT-1132 appeared to be structurally related to the AT from thermophilic archaea Geoglobus acetivorans. Thus, we have identified and characterized PLP fold type IV ATs that were active toward both amino acids and a variety of (R)-amines. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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16 pages, 2615 KiB

Open AccessEditor’s ChoiceArticle

Improving Effects of Laccase-Mediated Pectin–Ferulic Acid Conjugate and Transglutaminase on Active Peptide Production in Bovine Lactoferrin Digests

by Mingxia Xing, Ying Ji, Lianzhong Ai, Fan Xie, Yan Wu and Phoency F. H. Lai

Catalysts 2023, 13(3), 521; https://doi.org/10.3390/catal13030521 - 3 Mar 2023

Viewed by 1724

Abstract

Bovine lactoferrin (bLf) is a multifunctional glycoprotein and a good candidate for producing diverse bioactive peptides, which are easily lost during over-digestion. Accordingly, the effects of laccase-mediated pectin–ferulic acid conjugate (PF) and transglutaminase (TG) on improving the production of bLf active peptides by in vitro gastrointestinal digestion were investigated. Using ultra-high-performance liquid chromatography tandem mass spectroscopy (UPLC-MS-MS), the digests of bLf alone, PF-encapsulated bLf complex (LfPF), and TG-treated LfPF complex (LfPFTG) produced by conditioned in vitro gastric digestion (2000 U/mL pepsin, pH 3.0, 37 °C, 2 h) were identified with seven groups of active peptide-related fragments, including three common peptides (VFEAGRDPYKLRPVAAE, FENLPEKADRDQYEL, and VLRPTEGYL) and four differential peptides (GILRPYLSWTE, ARSVDGKEDLIWKL, YLGSRYLT, and FKSETKNLL). The gastric digest of LfPF contained more diverse and abundant detectable peptides of longer lengths than those of bLf and LfPFTG. After further in vitro intestinal digestion, two active peptide-related fragments (FEAGRDPYK and FENLPEKADRDQYE) remained in the final digest of LfPFTG; one (EAGRDPYKLRPVA) remained in that of bLf alone, but none remained in that of LfPF. Conclusively, PF encapsulation enhanced the production of bLf active peptide fragments under the in vitro gastric digestion applied. TG treatment facilitated active peptide FENLPEKADRDQYE being kept in the final gastrointestinal digest. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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19 pages, 3527 KiB

Open AccessArticle

Interaction of Jania rubens Polyphenolic Extract as an Antidiabetic Agent with α-Amylase, Lipase, and Trypsin: In Vitro Evaluations and In Silico Studies

by Asmaa Nabil-Adam, Mohamed L. Ashour, Tamer M. Tamer, Mohamed A. Shreadah and Mohamed A. Hassan

Catalysts 2023, 13(2), 443; https://doi.org/10.3390/catal13020443 - 18 Feb 2023

Cited by 18 | Viewed by 3187

Abstract

Jania rubens red seaweed has various bioactive compounds that can be used for several medicinal and pharmaceutical applications. In this study, we investigate the antidiabetic, anti-inflammatory, and antioxidant competency of Jania rubens polyphenolic extract (JRPE) by assessing their interactions with α-amylase, lipase, and trypsin enzymes. HPLC analysis revealed the dominance of twelve polyphenolic compounds. We performed computational analysis using α-amylase, lipase, and trypsin as target proteins for the polyphenols to explore their activities based on their predicted modes of binding sites following molecular modeling analysis. The molecular docking analysis demonstrated a good affinity score with a noticeable affinity to polyphenolic compositions of Jania rubens. The compounds with the highest affinity score for α-amylase (PDB: 4W93) were kaempferol, quercetin, and chlorogenic acid, with −8.4, −8.8 and −8 kcal/mol, respectively. Similarly, lipase (PDB: 1LPB) demonstrated high docking scores of −7.1, −7.4, and −7.2 kcal/mol for kaempferol, quercetin, and chlorogenic acid, respectively. Furthermore, for trypsin (PDB: 4DOQ) results, kaempferol, quercetin, and chlorogenic acid docking scores were −7.2, −7.2, and −7.1 kcal/mol, respectively. The docking findings were verified using in vitro evaluations, manifesting comparable results. Overall, these findings enlighten that the JRPE has antidiabetic, anti-inflammatory, and antioxidant properties using different diabetics’ enzymes that could be further studied using in vivo investigations for diabetes treatment. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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10 pages, 5401 KiB

Open AccessEditor’s ChoiceCommunication

Bienzymatic Cascade Combining a Peroxygenase with an Oxidase for the Synthesis of Aromatic Aldehydes from Benzyl Alcohols

by Yunjian Ma, Zongquan Li, Hao Zhang, Vincent Kam Wai Wong, Frank Hollmann and Yonghua Wang

Catalysts 2023, 13(1), 145; https://doi.org/10.3390/catal13010145 - 8 Jan 2023

Cited by 4 | Viewed by 2343

Abstract

Aromatic aldehydes are important aromatic compounds for the flavour and fragrance industry. In this study, a parallel cascade combining aryl alcohol oxidase from Pleurotus eryngii (PeAAOx) and unspecific peroxygenase from the basidiomycete Agrocybe aegerita (AaeUPO) to convert aromatic primary alcohols into high-value aromatic aldehydes is proposed. Key influencing factors in the process of enzyme cascade catalysis, such as enzyme dosage, pH and temperature, were investigated. The universality of PeAAOx coupled with AaeUPO cascade catalysis for the synthesis of aromatic aldehyde flavour compounds from aromatic primary alcohols was evaluated. In a partially optimised system (comprising 30 μM PeAAOx, 2 μM AaeUPO at pH 7 and 40 °C) up to 84% conversion of 50 mM veratryl alcohol into veratryl aldehyde was achieved in a self-sufficient aerobic reaction. Promising turnover numbers of 2800 and 21,000 for PeAAOx and AaeUPO, respectively, point towards practical applicability. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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13 pages, 1657 KiB

Open AccessArticle

Optimized Conditions for Preparing a Heterogeneous Biocatalyst via Cross-Linked Enzyme Aggregates (CLEAs) of β-Glucosidase from Aspergillus niger

by Thiago M. da Cunha, Adriano A. Mendes, Daniela B. Hirata and Joelise A. F. Angelotti

Catalysts 2023, 13(1), 62; https://doi.org/10.3390/catal13010062 - 28 Dec 2022

Cited by 2 | Viewed by 1636

Abstract

This study mainly aims to find the optimal conditions for immobilizing a non-commercial β-glucosidase from Aspergillus niger via cross-linked enzyme aggregates (CLEAs) by investigating the effect of cross-linking agent (glutaraldehyde) concentration and soy protein isolate/enzyme ratio (or spacer/enzyme ratio) on the catalytic performance of β-glucosidase through the central composite rotatable design (CCRD). The influence of certain parameters such as pH and temperature on the hydrolytic activity of the resulting heterogeneous biocatalyst was assessed and compared with those of a soluble enzyme. The catalytic performance of both the soluble and immobilized enzyme was assessed by hydrolyzing

ρ

-nitrophenyl-β-D-glucopyranoside (

ρ

-NPG) at pH 4.5 and 50 °C. It was found that there was a maximum recovered activity of around 33% (corresponding to hydrolytic activity of 0.48 U/mL) in a spacer/enzyme ratio of 4.69 (mg/mg) using 25.5 mM glutaraldehyde. The optimal temperature and pH conditions for the soluble enzyme were 60 °C and 4.5, respectively, while those for CLEAs of β-glucosidase were between 50 and 65 °C and pH 3.5 and 4.0. These results reveal that the immobilized enzyme is more stable in a wider pH and temperature range than its soluble form. Furthermore, an improvement was observed in thermal stability after immobilization. After 150 days at 4 °C, the heterogeneous biocatalyst retained 80% of its original activity, while the soluble enzyme retained only 10%. The heterogeneous biocatalyst preparation was also characterized by TG/DTG and FT-IR analyses that confirmed the introduction of carbon chains via cross-linking. Therefore, the immobilized biocatalyst prepared in this study has improved enzyme stabilization, and it is an interesting approach to preparing heterogeneous biocatalysts for industrial applications. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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14 pages, 1308 KiB

Open AccessArticle

Application of Endoxylanases of Bacillus halodurans for Producing Xylooligosaccharides from Empty Fruit Bunch

by Chanakan Thirametoakkhara, Yi-Cheng Hong, Nuttapol Lerkkasemsan, Jian-Mao Shih, Chien-Yen Chen and Wen-Chien Lee

Catalysts 2023, 13(1), 39; https://doi.org/10.3390/catal13010039 - 25 Dec 2022

Cited by 5 | Viewed by 2030

Abstract

Endo-1,4-β-xylanase catalyzes the random hydrolysis of β-1,4-D-xylosidic bonds in xylan, resulting in the formation of oligomers of xylose. This study aims to demonstrate the promise of endoxylanases from alkaliphilic Bacillus halodurans for the production of xylooligosaccharides (XOS) from oil palm empty fruit bunch (EFB) at high pH. Two enzyme preparations were employed: recombinant endoxylanase Xyn45 (GH10 xylanase) and nonrecombinant endoxylanases, a mixture of two extracellular endo-1,4-β-xylanases Xyn45 and Xyn23 (GH11 xylanase) produced by B. halodurans. EFB was first treated with an alkaline solution. Then, the dissolved xylan-containing fraction was retained, and a prepared enzyme was added to react at pH 8 to convert xylan into XOS. Compared with the use of only Xyn45, the combined use of Xyn45 and Xyn23 resulted in a higher yield of XOS, suggesting the synergistic effect of the two endoxylanases. The yield of XOS obtained from EFB was as high as 46.77% ± 1.64% (w/w), with the xylobiose-to-xylotriose ratio being 6:5. However, when the enzyme activity dose was low, the product contained more xylotriose than xylobiose. Four probiotic lactobacilli and bifidobacteria grew well on a medium containing XOS from EFB. The presence of XOS increased cell mass and reduced pH, suggesting that XOS promoted the growth of probiotics. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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21 pages, 4378 KiB

Open AccessArticle

Immobilization of Recombinant Endoglucanase (CelA) from Clostridium thermocellum on Modified Regenerated Cellulose Membrane

by Zi-Han Weng, Parushi Nargotra, Chia-Hung Kuo and Yung-Chuan Liu

Catalysts 2022, 12(11), 1356; https://doi.org/10.3390/catal12111356 - 3 Nov 2022

Cited by 12 | Viewed by 1988

Abstract

Cellulases are being widely employed in lignocellulosic biorefineries for the sustainable production of value-added bioproducts. However, the high production cost, sensitivity, and non-reusability of free cellulase enzymes impede their commercial applications. Enzyme immobilization seems to be a potential approach to address the aforesaid complications. The current study aims at the production of recombinant endoglucanase (CelA) originated from the cellulosome of Clostridium thermocellum in Escherichia coli (E. coli), followed by immobilization using modified regenerated cellulose (RC) membranes. The surface modification of RC membranes was performed in two different ways: one to generate the immobilized metal ion affinity membranes RC-EPI-IDA-Co²⁺ (IMAMs) for coordination coupling and another to develop aldehyde functional group membranes RC-EPI-DA-GA (AMs) for covalent bonding. For the preparation of IMAMs, cobalt ions expressed the highest affinity effect compared to other metal ions. Both enzyme-immobilized membranes exhibited better thermal stability and maintained an improved relative activity at higher temperatures (50–90 °C). In the storage analysis, 80% relative activity was retained after 15 days at 4 °C. Furthermore, the IMAM- and AM-immobilized CelA retained 63% and 53% relative activity, respectively, after being reused five times. As to the purification effect during immobilization, IMAMs showed a better purification fold of 3.19 than AMs. The IMAMs also displayed better kinetic parameters, with a higher Vmax of 15.57 U mg⁻¹ and a lower Km of 36.14 mg mL⁻¹, than those of AMs. The IMAMs were regenerated via treatment with stripping buffer and reloaded with enzymes and displayed almost 100% activity, the same as free enzymes, up to 5 cycles of regeneration. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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17 pages, 1061 KiB

Open AccessArticle

Production and Characterization of Durvillaea antarctica Enzyme Extract for Antioxidant and Anti-Metabolic Syndrome Effects

by Ming-Kuei Shih, Chih-Yao Hou, Cheng-Di Dong, Anil Kumar Patel, Yung-Hsiang Tsai, Mei-Chun Lin, Zheng-Ying Xu, Pitchurajan Krishna Perumal, Chia-Hung Kuo and Chun-Yung Huang

Catalysts 2022, 12(10), 1284; https://doi.org/10.3390/catal12101284 - 21 Oct 2022

Cited by 7 | Viewed by 2156

Abstract

In this study, three enzyme hydrolysate termed Dur-A, Dur-B, and Dur-C, were produced from Durvillaea antarctica biomass using viscozyme, cellulase, and α-amylase, respectively. Dur-A, Dur-B, and Dur-C, exhibited fucose-containing sulfated polysaccharide from chemical composition determination and characterization by FTIR analyses. In addition, Dur-A, Dur-B, and Dur-C, had high extraction yields and low molecular weights. All extracts determined to have antioxidant activities by DPPH (2,2-diphenyl-1-picrylhydrazyl), ABTS (2,20-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt), and ferrous ion-chelating methods. All extracts were also able to positively suppress the activities of key enzymes involved in metabolic syndrome: angiotensin I-converting enzyme (ACE), α-amylase, α-glucosidase, and pancreatic lipase. In general, Dur-B exhibited higher antioxidant and higher anti-metabolic syndrome effects as compared to the other two extracts. Based on the above health promoting properties, these extracts (especially Dur-B) can be used as potential natural antioxidants and natural anti-metabolic syndrome agents in a variety of food, cosmetic, and nutraceutical products for health applications. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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Review

Jump to: Editorial, Research

23 pages, 1910 KiB

Open AccessReview

Natural Sun-Screening Compounds and DNA-Repair Enzymes: Photoprotection and Photoaging

by Amit Gupta, Ashish P. Singh, Varsha K. Singh, Prashant R. Singh, Jyoti Jaiswal, Neha Kumari, Vijay Upadhye, Suresh C. Singh and Rajeshwar P. Sinha

Catalysts 2023, 13(4), 745; https://doi.org/10.3390/catal13040745 - 13 Apr 2023

Cited by 10 | Viewed by 5474

Abstract

Ultraviolet radiation (UVR) has been scientifically proven to cause skin disorders such as sunburn, skin cancer and the symptoms of chronic exposure. Natural sun screening compounds have recently gained tremendous attention from the cosmetic and cosmeceutical sectors for treating skin disorders such as hyperpigmentation and aging. A wide range of natural UV-absorbing compounds have been used to replace or reduce the number of synthetic sunscreen molecules. One of the primary causes of photoaging is DNA damage, mainly caused by UVR. Photoprotection provided by traditional sunscreens is purely preventative and has no efficacy after DNA damage has been initiated. As a result, the quest for DNA-repair mechanisms that block, reverse, or postpone pathologic processes in UV-exposed skin has stimulated anti-photoaging research and methods to increase the effectiveness of traditional sunscreens. This review summarizes many natural compounds from microalgae, lichens, and plants that have demonstrated potential photoprotection effects against UV radiation-induced skin damage. Furthermore, it offers an overview of current breakthroughs in DNA-repair enzymes utilized in sunscreens and their influence on photoaging. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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23 pages, 2342 KiB

Open AccessReview

Agro-Industrial Food Waste as a Low-Cost Substrate for Sustainable Production of Industrial Enzymes: A Critical Review

by Vishal Sharma, Mei-Ling Tsai, Parushi Nargotra, Chiu-Wen Chen, Chia-Hung Kuo, Pei-Pei Sun and Cheng-Di Dong

Catalysts 2022, 12(11), 1373; https://doi.org/10.3390/catal12111373 - 5 Nov 2022

Cited by 76 | Viewed by 13141

Abstract

The grave environmental, social, and economic concerns over the unprecedented exploitation of non-renewable energy resources have drawn the attention of policy makers and research organizations towards the sustainable use of agro-industrial food and crop wastes. Enzymes are versatile biocatalysts with immense potential to transform the food industry and lignocellulosic biorefineries. Microbial enzymes offer cleaner and greener solutions to produce fine chemicals and compounds. The production of industrially important enzymes from abundantly present agro-industrial food waste offers economic solutions for the commercial production of value-added chemicals. The recent developments in biocatalytic systems are designed to either increase the catalytic capability of the commercial enzymes or create new enzymes with distinctive properties. The limitations of low catalytic efficiency and enzyme denaturation in ambient conditions can be mitigated by employing diverse and inexpensive immobilization carriers, such as agro-food based materials, biopolymers, and nanomaterials. Moreover, revolutionary protein engineering tools help in designing and constructing tailored enzymes with improved substrate specificity, catalytic activity, stability, and reaction product inhibition. This review discusses the recent developments in the production of essential industrial enzymes from agro-industrial food trash and the application of low-cost immobilization and enzyme engineering approaches for sustainable development. Full article

(This article belongs to the Special Issue Enzymes in Biomedical, Cosmetic and Food Application)

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