Isolation and characterization of a halotolerant and protease-resistant α-galactosidase from the gut metagenome of Hermetia illucens

Lee, Chang-Muk; Kim, Su-Yeon; Song, Jae-Eun; Lee, Youngseok; Sim, Ji Hyun; Hahn, Bum‐Soo

doi:10.1016/j.jbiotec.2018.05.003

Cited by 25 publications

(12 citation statements)

References 31 publications

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“…Little is known about the microbial metabolism taking place in the larval guts, since past studies have mostly focused on clarifying phylogenetic dynamics in relation to larval diet. Detailed investigations of metabolic processes taking place in larvae and attempts to exploit them for biotechnological applications are sparse (Lee et al, 2018;Song et al, 2018;Zhan et al, 2019). Tools imputing metagenomes to 16S rRNA gene-based amplicon data such as PICRUSt (Langille et al, 2013) or Tax4Fun (Aßhauer et al, 2015) have been used to provide insights into functional genes.…”

Section: Introductionmentioning

confidence: 99%

Impact of Processed Food (Canteen and Oil Wastes) on the Development of Black Soldier Fly (Hermetia illucens) Larvae and Their Gut Microbiome Functions

et al. 2021

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Canteens represent an essential food supply hub for educational institutions, companies, and business parks. Many people in these locations rely on a guaranteed service with consistent quality. It is an ongoing challenge to satisfy the demand for sufficient serving numbers, portion sizes, and menu variations to cover food intolerances and different palates of customers. However, overestimating this demand or fluctuating quality of dishes leads to an inevitable loss of unconsumed food due to leftovers. In this study, the food waste fraction of canteen leftovers was identified as an optimal diet for black soldier fly (Hermetia illucens) larvae based on 50% higher consumption and 15% higher waste reduction indices compared with control chicken feed diet. Although the digestibility of food waste was nearly twice as high, the conversion efficiency of ingested and digested chicken feed remains unparalleled (17.9 ± 0.6 and 37.5 ± 0.9 in CFD and 7.9 ± 0.9 and 9.6 ± 1.0 in FWD, respectively). The oil separator waste fraction, however, inhibited biomass gain by at least 85% and ultimately led to a larval mortality of up to 96%. In addition to monitoring larval development, we characterized physicochemical properties of pre- and post-process food waste substrates. High-throughput amplicon sequencing identified Firmicutes, Proteobacteria, and Bacteroidota as the most abundant phyla, and Morganella, Acinetobacter, and certain Lactobacillales species were identified as indicator species. By using metagenome imputation, we additionally gained insights into the functional spectrum of gut microbial communities. We anticipate that the results will contribute to the development of decentralized waste-management sites that make use of larvae to process food waste as it has become common practice for biogas plants.

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Section: Introductionmentioning

confidence: 99%

Impact of Processed Food (Canteen and Oil Wastes) on the Development of Black Soldier Fly (Hermetia illucens) Larvae and Their Gut Microbiome Functions

et al. 2021

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“…BSF larvae are voracious consumers and generalist saprophagous insects [5]; therefore, the larvae have been used to bio-convert a wide range of organic waste, including food processing residue, food waste, crop straw and animal manure [6–9]. The harvested larvae are exploitable for the isolation of bioactive substances (e.g., hydrolase [10, 11], antimicrobial peptides [12] and chitin [13]). Moreover, the larvae of BSF are rich in lipids and proteins, which can be used as feed or as ingredients for poultry, livestock and aquaculture [5, 14, 15].…”

Section: Introductionmentioning

confidence: 99%

Reference gene selection for quantitative gene expression analysis in black soldier fly (Hermetia illucens)

2019

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Hermetia illucens is an important resource insect for the conversion of organic waste. Quantitative PCR (qPCR) is the primary tool of gene expression analysis and a core technology of molecular biology research. Reference genes are essential for qPCR analysis; however, a stability analysis of H . illucens reference genes has not yet been carried out. To find suitable reference genes for normalizing gene expression data, the stability of eight housekeeping genes (including ATP6V1A , RPL8 , EF1 , Tubulin , TBP , GAPDH , Actin and RP49 ) was investigated under both biotic (developmental stages, tissues and sex) and abiotic (heavy metals, food, antibiotics) conditions. Gene expression data were analysed by geNorm, NormFinder, BestKeeper, and ΔCt programs. A set of specific reference genes was recommended for each experimental condition using the results of RefFinder synthesis analysis. This study offers a solid foundation for further studies of the molecular biology of H . illucens .

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“…α‐Galactosidases have applications in the food industry for removal of RFOs from various legumes and beans; in the beet‐sugar industry for removal of raffinose from beet sugar; and in the feed industry for improving the nutritional value of animal feed (Boopathy, Gupta, & Ramudu, ; Moon et al, ; Zhou et al, ). Microbial α‐galactosidases are particularly widely applied in the food industries owing to their biochemical properties and catalytic efficiencies (Chauhan, Kumar, Siddiqi, & Sharma, ; Huang et al, ; Katrolia et al, ; Lee et al, ; Wang et al, ). α‐Galactosidases from various microorganisms have been shown to degrade RFOs from soy milk (Ferreira et al, ; Huang et al, ; Jang et al, ; Katrolia et al, ; Saad & Fawzi, ).…”

Section: Introductionmentioning

confidence: 99%

Enhanced elimination of non‐digestible oligosaccharides from soy milk by immobilized α‐galactosidase: A comparative analysis

Katrolia

Liu

et al. 2019

J Food Biochem

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This study compared two immobilization matrices like calcium‐alginate and chitosan for immobilization of α‐galactosidase and evaluated their potential for the removal of non‐digestible raffinose family oligosaccharides from soy milk which cause abdominal discomfort. The pH optima of the free and immobilized enzymes were found to be similar at pH 4.0. The chitosan‐immobilized α‐galactosidase displayed higher optimal temperature (60°C) compared to alginate‐immobilized enzyme (45°C) and free enzyme (50°C). The chitosan‐immobilized and alginate‐immobilized α‐galactosidases displayed 93.7% and 97.6% hydrolysis of raffinose family oligosaccharides, respectively, while the free enzyme hydrolyzed only 30.3% oligosaccharides present in soy milk in 4 hr. Remarkably, both the immobilized enzymes showed complete removal of raffinose family oligosaccharides in 8 hr. Moreover, reusability studies indicate that even after five cycles of reuse, the chitosan and alginate‐immobilized enzymes displayed 99% and 60% hydrolysis, respectively. Practical applications In this study, we have used two inexpensive and non‐toxic matrices for immobilizing α‐galactosidase. We report that entrapment of α‐galactosidase with chitosan significantly improved the optimal temperature of α‐galactosidase, which is advantageous in food industry. The hydrolysis of raffinose family oligosaccharides in soy milk was also greatly enhanced after immobilization with chitosan and alginate. Thus, the results described in this study have relevance for development of safe, cost‐effective and efficient method for removal of non‐digestible soy oligosaccharides in food industry.

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Isolation and characterization of a halotolerant and protease-resistant α-galactosidase from the gut metagenome of Hermetia illucens

Cited by 25 publications

References 31 publications

Impact of Processed Food (Canteen and Oil Wastes) on the Development of Black Soldier Fly (Hermetia illucens) Larvae and Their Gut Microbiome Functions

Impact of Processed Food (Canteen and Oil Wastes) on the Development of Black Soldier Fly (Hermetia illucens) Larvae and Their Gut Microbiome Functions

Reference gene selection for quantitative gene expression analysis in black soldier fly (Hermetia illucens)

Enhanced elimination of non‐digestible oligosaccharides from soy milk by immobilized α‐galactosidase: A comparative analysis

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