Food Enzymes From Extreme Environments: Sources and Bioprocessing

Akanbi, Taiwo O.; Agyei, Dominic; Saari, Nazamid

doi:10.1016/b978-0-12-813280-7.00046-3

Cited by 8 publications

(6 citation statements)

References 146 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Medically, hot springs are known to relieve musculoskeletal problems (Vaidya & Nakarmi 2020). Although there is no direct evidence on the medical effectiveness of hot springs, documentation showed a great number of microbial enzymes isolated from these water sources that may explain the partial, although still inconclusive, medicinal effects to the body (Akanbi et al 2019). In a biological aspect, hot springs are home to several thermophilic organisms such as prokaryotes of different types (Castenholz 2009;Dodds & Whiles 2010), viruses (Wirth et al 2021), nematodes (Poinar 2015), and a group of protozoans known as free-living amoebae (FLA) (Marciano-Cabral & Cabral 2007;Visvesvara 2010).…”

Section: Introductionmentioning

confidence: 99%

Current report on the prevalence of free-living amoebae (FLA) in natural hot springs: a systematic review

Fabros

Diesta

Oronan

et al. 2021

Journal of Water and Health

View full text Add to dashboard Cite

The occurrence of potentially pathogenic free-living amoebae (FLA) in natural hot springs is considered a public health concern. FLAs are known to cause serious health outcomes to a wide spectrum of mammalian hosts. The present study aimed to provide the distribution of isolated cases of FLAs in hot springs through a systematic review process of available published articles online. Relevant studies are published between January 2010 and January 2020 involving the isolation of Naegleria spp., Acanthamoeba spp., Balamuthia spp., Sappinia spp., and Vermamoeba spp. in natural hot springs in the United States, South America, North America, Europe, Asia, and Africa. Articles were identified through a search of PubMed and Google Scholar databases. Out of 94 articles screened, a total of 20 articles are included in the study with consideration of established inclusion and exclusion criteria. The most common FLAs isolated in hot springs are Acanthamoeba spp. (134; 48.5%) and Naegleria spp. (127; 46.0%). Other FLAs isolated in hot springs include Balamuthia spp. (2; 0.7%) and Vermamoeba spp. (13; 4.7%). FLA in hot springs used for recreational and medical purposes is a potential source of infection. It is recommended that strict surveillance and maintenance of hot springs be implemented to prevent potential future infection.

show abstract

Section: Introductionmentioning

confidence: 99%

Current report on the prevalence of free-living amoebae (FLA) in natural hot springs: a systematic review

Fabros

Diesta

Oronan

et al. 2021

Journal of Water and Health

View full text Add to dashboard Cite

show abstract

“…Scientists globally are delving into genetic alterations of microorganisms possessing advantageous industrial attributes, specifically focusing on heatresistant enzymes sourced from thermophilic bacilli, which find diverse applications in the commercial sphere (Margaryan et al, 2018). Hot springs are renowned for housing an abundant reservoir of microbial enzymes, encompassing lipases, proteases, and cellulases (Akanbi et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Thermostable Amylase from Cytobacillus firmus: Characterization, Optimization, and Implications in Starch Hydrolysis

Al-Harthy,

Hozzein,

Abdelkader

et al. 2024

Egypt. J. Microbiol.

View full text Add to dashboard Cite

H OT springs are known to be rich in diverse microorganisms, including thermophilic bacteria capable of producing industrially important enzymes. This study aimed to isolate, purify, and identify thermophilic bacteria from three hot springs located in the southern region of Saudi Arabia, namely Al-Ma'a Al-Har, Al-Aredhah, and Al-Ahsarai hot spring. The isolated bacterial isolates were screened for amylase enzyme production, and the most potent isolate, Cytobacillus firmus OQ834432 isolate OHA8, was selected for large-scale production of the amylase enzyme. The enzyme was then purified using salt precipitation, Sephacryl S-200 chromatography, and DEAE-Sepharose column chromatography. A total of twenty-one bacterial species were identified, with Cytobacillus firmus exhibiting the highest amylase activity. The optimal conditions for the amylase enzyme activity were found to be at 50°C and pH 5.0, with a 153% enhancement in activity in the presence of magnesium ions. The enzyme's activity was inhibited by EDTA and was found to be active with starch and amylopectin at 100% and 110.3%, respectively. In conclusion, this study demonstrates the potential of thermophilic bacteria from hot springs to produce industrially important enzymes and provides insights into the optimal conditions for enzyme production and activity. These findings have significant implications for the development of biotechnological applications utilizing thermophilic bacteria in various industrial sectors.

show abstract

“…So, a suitable way to decrease production costs is to produce high-value products such as peptides, omega-3 fatty acids, sulfated polysaccharides, and enzymes [4]. Moreover, these products may be worth much more than their original products [2,5]. Due to the high concentration of digestive enzymes in marine animals' viscera, which make up a large part of their by-products, researchers and industry attention has been drawn to the extraction and puri cation of enzymes, especially aspartic proteases (pepsin) in the stomach and serine proteases (trypsin, chymotrypsin, collagenase, and elastase) in the viscera [2,5].…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, marine enzymes have demonstrated excellent activity across different temperatures and pH ranges compared to enzymes derived from land animals [7]. In this regard, various methods have been used to extract, purify, and identify enzymes, including ammonium sulfate precipitation, gel ltration, anion exchange chromatography, and polyacrylamide gel electrophoresis [5,6]. In this regard, various methods have been used to extract, purify, and identify enzymes, including ammonium sulfate precipitation, gel ltration, anion exchange chromatography, and polyacrylamide gel electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, these products may be worth much more than their original products [2,5]. Due to the high concentration of digestive enzymes in marine animals' viscera, which make up a large part of their by-products, researchers and industry attention has been drawn to the extraction and puri cation of enzymes, especially aspartic proteases (pepsin) in the stomach and serine proteases (trypsin, chymotrypsin, collagenase, and elastase) in the viscera [2,5]. Pepsin, which is created by changes in the pepsinogen structure when it is exposed to hydrochloric acid (HCl), is a marine enzyme that belongs to the class of aspartic proteases isolated from various sources, which are used in a wide variety of industrial processes, such as collagen extraction, cheese production, sh silage production, sh processing, and medical research [5,6].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

View full text Add to dashboard Cite

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.

show abstract

Food Enzymes From Extreme Environments: Sources and Bioprocessing

Cited by 8 publications

References 146 publications

Current report on the prevalence of free-living amoebae (FLA) in natural hot springs: a systematic review

Current report on the prevalence of free-living amoebae (FLA) in natural hot springs: a systematic review

Thermostable Amylase from Cytobacillus firmus: Characterization, Optimization, and Implications in Starch Hydrolysis

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

Contact Info

Product

Resources

About