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Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry
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Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Food Chemistry".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 8964

Special Issue Editors

Dr. Hong Jiang

E-Mail Website
Guest Editor
College of Food Science and Engineering, Ocean University of China, Qingdao, China
Interests: food synthetic biology
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Zhipeng Wang

E-Mail Website
Co-Guest Editor
School of Marine Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China
Interests: marine enzyme engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

For a long time, enzymes have played a vital role in biocatalysis. As is well known, the biotechnological tool of enzymes not only is specific and safe but also has the characteristics of high efficiency and environmental friendliness. Therefore, the application of enzymes in the biomedicine, cosmetic, and food industry has received increasing attention. At present, enzymes, including glycosyl transferase, glycoside hydrolases, lipases, proteases, catalase, laccase, lysozyme, superoxide dismutase, and so on, have been used in different segments, such as food processing, food preservation, food control, pharmaceutical ingredient extraction, pharmaceutical production, pathogens detection, and cosmetics production. However, compared with the abundant enzyme resources in nature, relatively few enzymes are used in the above industries. As a consequence, the mining of enzymes with high activity, improvement of enzyme stability based on rational design, construction of robust enzyme expression systems, and establishment of high-efficiency catalysis systems and technology are of great significance to promote the application of enzymes in the biomedicine, cosmetic, and food industry. This Special Issue aims to collect papers on aspects related to enzyme mining, expression, design, and application in food, biomedicine, and cosmetic segments. In this Special Issue, both original research articles and reviews are welcome and encouraged.

Dr. Hong Jiang
Prof. Dr. Zhipeng Wang
Guest Editors

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Keywords

  • enzyme cloning and expression
  • rational design
  • enzyme techniques
  • robust enzyme expression
  • food processing
  • food preservation
  • food control
  • food testing and analysis
  • pharmaceutical ingredient extraction
  • pharmaceutical production
  • cosmetics production

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Published Papers (6 papers)

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Research

15 pages, 5457 KiB  
Article
Display of Bacterial Exochitanase on Bacillus subtilis Spores Improved Enzyme Stability and Recyclability
by Mati Ullah, Yutong Xia, Dalal Sulaiman Alshaya, Jianda Han, Kotb A. Attia, Tawaf Ali Shah and Huayou Chen
Molecules 2024, 29(18), 4302; https://doi.org/10.3390/molecules29184302 - 11 Sep 2024
Viewed by 396
Abstract
Chitin is the second most prevalent polysaccharide found in nature, following cellulose. Amino-oligosaccharides, the byproducts of chitin degradation, exhibit favorable biological properties and potential for various uses. Chitinases play a crucial function in the breakdown of chitin, and their exceptionally effective production has [...] Read more.
Chitin is the second most prevalent polysaccharide found in nature, following cellulose. Amino-oligosaccharides, the byproducts of chitin degradation, exhibit favorable biological properties and potential for various uses. Chitinases play a crucial function in the breakdown of chitin, and their exceptionally effective production has garnered significant interest. Here, in this study, the exochitinase PbChiA, obtained from Paenibacillus barengoltzii, was recombinantly produced and immobilized using the CotG surface protein of Bacillus subtilis WB800N. The resulting strain Bacillus subtilis WB800N pHS-CotG-Chi exhibited exceptional heat stability and efficacy across various pH levels. The chitinolytic activity of the enzyme, which had been isolated and immobilized on the spore surface, was measured to be approximately 16.06 U/mL. Including Ni2+, Zn+2, and K+, and EDTA at various concentration levels in the reaction system, has significantly enhanced the activity of the immobilized enzyme. The immobilized exochitinase demonstrated a notable rate of recycling, as the recombinant spores sustained a relative enzyme activity of more than 70% after three cycles and 62.7% after four cycles. These findings established a basis for additional investigation into the role and practical use of the immobilized bacterial exochitinase in industry. Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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14 pages, 1525 KiB  
Article
Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins
by El Hocine Siar, Pedro Abellanas-Perez, Javier Rocha-Martin and Roberto Fernandez-Lafuente
Molecules 2024, 29(15), 3674; https://doi.org/10.3390/molecules29153674 - 2 Aug 2024
Viewed by 491
Abstract
It has been reported that the modification of immobilized glyoxyl–ficin with aldehyde dextran can promote steric hindrances that greatly reduce the activity of the immobilized protease against hemoglobin, while the protease still maintained a reasonable level of activity against casein. In this paper, [...] Read more.
It has been reported that the modification of immobilized glyoxyl–ficin with aldehyde dextran can promote steric hindrances that greatly reduce the activity of the immobilized protease against hemoglobin, while the protease still maintained a reasonable level of activity against casein. In this paper, we studied if this effect may be different depending on the amount of ficin loaded on the support. For this purpose, both the moderately loaded and the overloaded glyoxyl–ficin biocatalysts were prepared and modified with aldehyde dextran. While the moderately loaded biocatalyst had a significantly reduced activity, mainly against hemoglobin, the activity of the overloaded biocatalyst was almost maintained. This suggests that aldehyde dextran was able to modify areas of the moderately loaded enzyme that were not available when the enzyme was overloaded. This modification promoted a significant increase in biocatalyst stability for both biocatalysts, but the stability was higher for the overloaded biocatalyst (perhaps due to a combination of inter- and intramolecular crosslinking). Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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19 pages, 5280 KiB  
Article
A Novel Cold-Adapted and High-Alkaline Alginate Lyase with Potential for Alginate Oligosaccharides Preparation
by Hai-Ying Wang, Zhi-Fang Chen, Zhi-Hong Zheng, Hui-Wen Lei, Hai-Hua Cong and Hai-Xiang Zhou
Molecules 2023, 28(17), 6190; https://doi.org/10.3390/molecules28176190 - 22 Aug 2023
Cited by 2 | Viewed by 1338
Abstract
Alginate oligosaccharides (AOs) prepared through enzymatic reaction by diverse alginate lyases under relatively controllable and moderate conditions possess versatile biological activities. But widely used commercial alginate lyases are still rather rare due to their poor properties (e.g., lower activity, worse thermostability, ion tolerance, [...] Read more.
Alginate oligosaccharides (AOs) prepared through enzymatic reaction by diverse alginate lyases under relatively controllable and moderate conditions possess versatile biological activities. But widely used commercial alginate lyases are still rather rare due to their poor properties (e.g., lower activity, worse thermostability, ion tolerance, etc.). In this work, the alginate lyase Alyw208, derived from Vibrio sp. W2, was expressed in Yarrowia lipolytica of food grade and characterized in order to obtain an enzyme with excellent properties adapted to industrial requirements. Alyw208 classified into the polysaccharide lyase (PL) 7 family showed maximum activity at 35 °C and pH 10.0, indicating its cold-adapted and high-alkaline properties. Furthermore, Alyw208 preserved over 70% of the relative activity within the range of 10–55 °C, with a broader temperature range for the activity compared to other alginate-degrading enzymes with cold adaptation. Recombinant Alyw208 was significantly activated with 1.5 M NaCl to around 2.1 times relative activity. In addition, the endolytic Alyw208 was polyG-preferred, but identified as a bifunctional alginate lyase that could degrade both polyM and polyG effectively, releasing AOs with degrees of polymerization (DPs) of 2–6 and alginate monomers as the final products (that is, DPs 1–6). Alyw208 has been suggested with favorable properties to be a potent candidate for biotechnological and industrial applications. Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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9 pages, 3691 KiB  
Communication
Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability
by Jing Jiang, Jing-Ling Deng, Zhi-Gang Wang, Xiao-Yu Chen, Shu-Jie Wang and Yong-Chuang Wang
Molecules 2023, 28(7), 3037; https://doi.org/10.3390/molecules28073037 - 29 Mar 2023
Cited by 4 | Viewed by 1590
Abstract
Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust [...] Read more.
Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust laccases has attracted significant attention. In this study, Vibrio sp. LA is a strain capable of producing cold-adapted laccases. The laccase coding gene L01 was cloned from this strain and expressed in Yarrowia lipolytica, a host with good secretion ability. The secreted L01 (approximate MW of 56,000 Da) had the activity and specific activity of 18.6 U/mL and 98.6 U/mg toward ABTS, respectively. The highest activity occurred at 35 °C. At 20 °C, L01 activity was over 70% of the maximum activity in pH conditions ranging from 4.5–10.0. Several synthetic dyes were efficiently degraded by L01. Owing to its robustness, salt tolerance, and pH stability, L01 is a promising catalytic tool for potential industrial applications. Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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16 pages, 20792 KiB  
Article
Screening and Characteristics of Marine Bacillus velezensis Z-1 Protease and Its Application of Enzymatic Hydrolysis of Mussels to Prepare Antioxidant Active Substances
by Jing Lu, Yu Zhao, Rong Hu, Yu Cheng, Junhuan Qin, Jie Yang, Yaowei Fang, Mingsheng Lyu and Shujun Wang
Molecules 2022, 27(19), 6570; https://doi.org/10.3390/molecules27196570 - 4 Oct 2022
Cited by 6 | Viewed by 2004
Abstract
Bacillus velezensis is a type of microorganism that is beneficial to humans and animals. In this work, a protease-producing B. velezensis strain Z-1 was screened from sludge in the sea area near Qingdao (deposit number CGMCC No. 25059). The response surface methodology [...] Read more.
Bacillus velezensis is a type of microorganism that is beneficial to humans and animals. In this work, a protease-producing B. velezensis strain Z-1 was screened from sludge in the sea area near Qingdao (deposit number CGMCC No. 25059). The response surface methodology was used to analyze protease production, and the optimal temperature was 37.09 °C and pH 7.73 with the addition of 0.42% NaCl, resulting in maximum protease production of 17.64 U/mL. The optimum reaction temperature and pH of the protease of strain Z-1 were 60 °C and 9.0, respectively. The protease had good temperature and pH stability, and good stability in solvents such as methanol, ethanol and Tween 80. Ammonium, NH4+,and Mn2+ significantly promoted enzyme activity, while Zn2+ significantly inhibited the enzyme activity. The protease produced by strain Z-1 was used for the enzymolysis of mussel meat. The mussel hydrolysate exhibited good antioxidant function, with a DPPH free radical removal rate of 75.3%, a hydroxyl free radical removal rate of 75.9%, and a superoxide anion removal rate of 84.4%. This study provides a reference for the application of B. velez protease and the diverse processing applications of mussel meat. Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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15 pages, 4206 KiB  
Article
A Novel Potent Crystalline Chitin Decomposer: Chitin Deacetylase from Acinetobacter schindleri MCDA01
by Guang Yang, Yuhan Wang, Yaowei Fang, Jia An, Xiaoyue Hou, Jing Lu, Rongjun Zhu and Shu Liu
Molecules 2022, 27(16), 5345; https://doi.org/10.3390/molecules27165345 - 22 Aug 2022
Cited by 10 | Viewed by 2389
Abstract
Chitosan is a functional ingredient that is widely used in food chemistry as an emulsifier, flocculant, antioxidant, or preservative. Chitin deacetylases (CDAs) can catalyze the hydrolysis of acetyl groups, making them useful in the clean production of chitosan. However, the high inactivity of [...] Read more.
Chitosan is a functional ingredient that is widely used in food chemistry as an emulsifier, flocculant, antioxidant, or preservative. Chitin deacetylases (CDAs) can catalyze the hydrolysis of acetyl groups, making them useful in the clean production of chitosan. However, the high inactivity of crystalline chitin catalyzed by CDAs has been regarded as the technical bottleneck of crystalline chitin deacetylation. Here, we mined the AsCDA gene from the genome of Acinetobacter schindleri MCDA01 and identified a member of the uraD_N-term-dom superfamily, which was a novel chitin deacetylase with the highest deacetylation activity. The AsCDA gene was expressed in Escherichia coli BL21 by IPTG induction, whose activity to colloidal chitin, α-chitin, and β-chitin reached 478.96 U/mg, 397.07 U/mg, and 133.27 U/mg, respectively. In 12 h, the enzymatic hydrolysis of AsCDA removed 63.05% of the acetyl groups from α-chitin to prepare industrial chitosan with a degree of deacetylation higher than 85%. AsCDA, as a potent chitin decomposer in the production of chitosan, plays a positive role in the upgrading of the chitosan industry and the value-added utilization of chitin biological resources. Full article
(This article belongs to the Special Issue Enzymes Applied in Biomedicine, Cosmetic, and Food Chemistry)
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