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Catalysts
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Biocatalysis in Food Technology and Processing
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Biocatalysis in Food Technology and Processing

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: closed (30 June 2020) | Viewed by 20944

Special Issue Editor

Prof. Dr. Francesco Secundo

E-Mail Website
Guest Editor
CNR, Istituto di Chimica del Riconoscimento Molecolare, I-20131 Milan, Italy
Interests: biocatalysis; protein conformation; analysis of food samples
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are commonly used in the food industry, in brewing, dairy processing, in oil and fat production, for the preparation of meat (or fish) products or of baking specialties. Beyond the well-established procedures to accelerate food processing, enzymes can also be employed to improve food properties such as digestibility and taste. Furthermore, they are increasingly applied for the biotransformation of wastes coming from the food industry, allowing the obtainment of products that might be re-employed in the food supply chain or used in other industrial applications, such as in the cosmetic or pharmaceutical field.

Besides food processing, biocatalysts are the most-commonly employed biological component in biosensors, which allow the detection of a variety of compounds, including undesired or even toxic molecules in food, thus contributing to monitoring food safety.

The use of enzymes to process food is thousands of years old and has now been renovated and endowed with new biotechnological tools. In this context, applied biocatalysis is an unavoidable and crucial technology to produce high quality and safe food products, satisfying new and increasing market demands.

This Special Issue of Catalysts aims at reporting new biocatalytic methodologies or biocatalysts exploitable in the food industry, expanding food science knowledge.

Prof. Francesco Secundo
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • biotrasformation
  • food
  • agricultural product
  • enzyme
  • biocatalyzed reaction
  • biosensor
  • nutrition

Published Papers (5 papers)

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Research

14 pages, 2023 KiB  
Article
Biocatalyzed Reactions towards Functional Food Components 4-Alkylcatechols and Their Analogues
by Ludmila Martínková, Romana Příhodová, Natalia Kulik, Helena Pelantová, Barbora Křístková, Lucie Petrásková and David Biedermann
Catalysts 2020, 10(9), 1077; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10091077 - 18 Sep 2020
Cited by 2 | Viewed by 2205
Abstract
Catechols are antioxidants and radical scavengers with a broad medical potential. 4-Methylcatechol (1b) and 4-ethylcatechol (2b) (occurring in some traditional fermented and smoked foods) activate the cell defense against oxidative stress. We examined the biocatalyzed reactions towards 4-n [...] Read more.
Catechols are antioxidants and radical scavengers with a broad medical potential. 4-Methylcatechol (1b) and 4-ethylcatechol (2b) (occurring in some traditional fermented and smoked foods) activate the cell defense against oxidative stress. We examined the biocatalyzed reactions towards 4-n-alkylcatechols with different side chains length, which is a factor important for the biological activities of catechols. 4-n-Alkylcatechols with methyl through heptyl side chains (1b–7b) were obtained in one pot by (i) oxidation of phenols 1a–7a with tyrosinase from Agaricus bisporus followed by (ii) reduction of ortho-quinones (intermediates) with L-ascorbic acid sodium salt. The conversions decreased with increasing side chain length. The preparative reactions were carried out with substrates 1a–5a. The isolated yields of the purified products decreased from 59% in 2b to 10% in 5b in correlation with logP of the substrates. Homology modeling indicated that the affinities of two tyrosinase isoforms (PPO3 and PPO4) to the substrates with side chains longer than C2 decreased with increasing side chain length. This was probably due to steric limitations and to missing interactions of the extended side chains in the active sites. We envisage using the model to predict further substrates of tyrosinase and testing the products, catechols, for radical-scavenging and biological activities. Full article
(This article belongs to the Special Issue Biocatalysis in Food Technology and Processing)
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13 pages, 1723 KiB  
Article
Expression and Characterization of a GH16 Family β-Agarase Derived from the Marine Bacterium Microbulbifer sp. BN3 and Its Efficient Hydrolysis of Agar Using Raw Agar-Producing Red Seaweeds Gracilaria sjoestedtii and Gelidium amansii as Substrates
by Ren Kuan Li, Xi Juan Ying, Zhi Lin Chen, Tzi Bun Ng, Zhi Min Zhou and Xiu Yun Ye
Catalysts 2020, 10(8), 885; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10080885 - 05 Aug 2020
Cited by 4 | Viewed by 2106
Abstract
Agarases catalyze the hydrolysis of agarose to oligosaccharides which display an array of biological and physiological functions with important industrial applications in health-related fields. In this study, the gene encoding agarase (Aga-ms-R) was cloned from Microbulbifer sp. BN3 strain. Sequence alignment indicated that [...] Read more.
Agarases catalyze the hydrolysis of agarose to oligosaccharides which display an array of biological and physiological functions with important industrial applications in health-related fields. In this study, the gene encoding agarase (Aga-ms-R) was cloned from Microbulbifer sp. BN3 strain. Sequence alignment indicated that Aga-ms-R belongs to the GH16 family and contains one active domain and two carbohydrate binding module (CBM) domains. The mature Aga-ms-R was expressed successfully by employing the Brevibacillus system. Purified rAga-ms-R was obtained with a specific activity of 100.75 U/mg. rAga-ms-R showed optimal activity at 50 °C and pH 7.0, and the enzyme activity was stable at 50 °C and also over the pH range of 5.0–9.0. After exposure of rAga-ms-R to 70 °C for 30 min, only partial enzyme activity remained. Thin layer chromatographic analysis of the enzymatic hydrolysate of agar obtained using rAga-ms-R disclosed that the hydrolysate comprised, in a long intermediate-stage of the hydrolysis reaction, mainly neoagarotetraose (NA4) and neoagarohexaose (NA6) but ultimately, predominantly neoagarotetraose and trace amounts of neoagarobiose (NA2). Hydrolysates of the raw red seaweeds Gracilaria sjoestedtii and Gelidium amansii, produced by incubation with rAga-ms-R, were mainly composed of neoagarotetraose. The results demonstrate the high efficiency of rAga-ms-R in producing neoagaraoligosaccharide under low-cost conditions. Full article
(This article belongs to the Special Issue Biocatalysis in Food Technology and Processing)
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16 pages, 2549 KiB  
Article
Soybean Protein Extraction by Alcalase and Flavourzyme, Combining Thermal Pretreatment for Enteral Feeding Product
by Truong Le Que Anh, Nguyen Thi Quynh Hoa, Pham Dinh Thanh Nguyen, Hoang Van Thanh, Pham Bao Nguyen, Le Thi Hong Anh and Dong Thi Anh Dao
Catalysts 2020, 10(8), 829; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10080829 - 23 Jul 2020
Cited by 14 | Viewed by 6839
Abstract
Soybean is one of the essential ingredients when formulating a tube feeding formula. In this study, we initially focused on determining which enzyme is suitable for hydrolyzing soy and comparing the soy protein enzymatic hydrolysis of three different enzymes at the same enzyme [...] Read more.
Soybean is one of the essential ingredients when formulating a tube feeding formula. In this study, we initially focused on determining which enzyme is suitable for hydrolyzing soy and comparing the soy protein enzymatic hydrolysis of three different enzymes at the same enzyme content: Flavourzyme, Protamex, and Alcalase. The result showed that Flavourzyme attained the highest soluble protein recovery efficiency (SPRE). Secondly, the study determined the effect of thermal treatment conditions such as thermal treatment duration, and then it showed that when combining the thermal treatment and enzymatic hydrolysis, the yield reached (61.44 ± 0.22)%, which was much higher than only using enzymatic hydrolysis (52.57 ± 0.27)%. Next, optimizing the enzymatic hydrolysis (combining thermal treatment) using Flavourzyme and Alcalase, Flavourzyme achieved (62.47 ± 0.12)%, while Alcalase attained (41.32 ± 0.13)%. The soy hydrolyzate using Flavourzyme achieved an average molecular size of 3.19 kDa at the following optimizing conditions: enzyme concentration, 16.09 U·g−1; pH, 7.02; temperature, 45.8 °C; and beans/water ratio, 1:3. In contrast, when using Alcalase, the soy hydrolyzate achieved an average molecular size of 1.52 kDa at the following optimizing conditions: enzyme concentration, 28.01 U·g−1; pH, 7.2; temperature, 56.5 °C; beans/water ratio, 1:4.6. Soy protein hydrolyzate of suitable viscosity and particle size flow through the inhaler with branched-chain amino acids achieved a BCAA (Branched Amino Acid) ratio of 2:1:1 for Alcalase and 4:1:1 for Flavourzyme. Soybean hydrolyzate using both enzymes attained a high SPRE and was suitable for the digestive ability of patients recovering from surgery. Soy protein is divided into amino acids, di- and tri-amino acids, and peptides to create a soluble protein source that helps feed patients with a sonde tube easily. In addition, the molecular weight of peptides will reduce viscosity significantly when passing through a sonde tube, preventing tube congestion. Full article
(This article belongs to the Special Issue Biocatalysis in Food Technology and Processing)
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12 pages, 3306 KiB  
Article
Effect of Pretreatment Methods on Enzymatic Kinetics of Ungelatinized Cassava Flour Hydrolysis
by Tien Cuong Nguyen, Son Chu-ky, Hong Nga Luong and Hai Van Nguyen
Catalysts 2020, 10(7), 760; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10070760 - 08 Jul 2020
Cited by 9 | Viewed by 2970
Abstract
The energy-saving glucose production process from starchy sources was developed by replacing high-temperature, liquid-phase by low-temperature, solid-phase. Therefore, the enzymatic hydrolysis under gelatinization temperature at very high gravity (≥300 g.L−1) of starchy substrates presents as an emerging technology. This study focused [...] Read more.
The energy-saving glucose production process from starchy sources was developed by replacing high-temperature, liquid-phase by low-temperature, solid-phase. Therefore, the enzymatic hydrolysis under gelatinization temperature at very high gravity (≥300 g.L−1) of starchy substrates presents as an emerging technology. This study focused on the hydrolysis kinetics of cassava flour affected by different pretreatment methods. Cassava flour (dried, milled) was prepared in acetate buffer (pH 4.2) with starch concentration ranging from 10–30% (w/w). The mash was then pre-treated by three different methods for 30 min using heating (30, 40, 50 °C), enzyme (Viscozyme L 0.1% w/w) and microwave (3 × 20 s at 800 W). The suspension was then hydrolyzed with Stargen 002 (0.2% w/w) at 30 °C for 48 h. The enzyme adsorption kinetics was described by the Langmuir isotherm equation. The pretreatments at 50 °C and with enzyme resulted in the highest efficiency with the hydrolysis yield ranging from 76–79% after 48 h. The hydrolysis yield decreased to 67% (using microwave), 66% (at 45 °C), 61% (at 40 °C) and 59% (at 30 °C). The linear relationship between enzyme adsorption and produced glucose was demonstrated. The kinetics of glucose production was fitted by an empirical equation (analogy with Michaelis-Menten model) and allowed predicting the maximum hydrolysis yield. Full article
(This article belongs to the Special Issue Biocatalysis in Food Technology and Processing)
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14 pages, 2031 KiB  
Article
Enzyme-Assisted Mechanical Peeling of Cassava Tubers
by Ziba Barati, Sajid Latif, Sebastian Romuli and Joachim Müller
Catalysts 2020, 10(1), 66; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10010066 - 02 Jan 2020
Cited by 4 | Viewed by 3422
Abstract
In this study, the effect of enzymatic pre-treatment and the size of cassava tubers on mechanical peeling was examined. Cassava tubers were sorted based on their mass as small, medium and large. Viscozyme® L and an abrasive cassava peeling machine was used [...] Read more.
In this study, the effect of enzymatic pre-treatment and the size of cassava tubers on mechanical peeling was examined. Cassava tubers were sorted based on their mass as small, medium and large. Viscozyme® L and an abrasive cassava peeling machine was used for the enzymatic pre-treatment and the mechanical peeling, respectively. Response surface methodology (RSM) was used to investigate the effect of the enzyme dose (0.5–1.9 mL g−1), incubation time (1.5–6 h), peeling time (1.5–4.5 min) and size of the tubers (small, medium and large) on the peeling process. Peeled surface area (PSA) and peel loss (PL) were measured as main responses in RSM. Results showed that the PSA and PL were significantly (p < 0.05) influenced by the enzyme dose, incubation time and peeling time. The size of tubers only had a significant impact on the PSA. The optimum operating conditions for different sizes of tubers were found and validated. Under optimum conditions, the PSA of the large tubers (89.52%) was significantly higher than the PSA of the medium and small tubers (p < 0.05). Application of enzymatic pre-treatment can improve the mechanical peeling process especially for larger cassava tubers. Full article
(This article belongs to the Special Issue Biocatalysis in Food Technology and Processing)
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