Enhancement of Amylase and Lipase Production from Bacillus licheniformis 016 Using Waste Chicken Feathers as Peptone Source

Baltaci, Mustafa Özkan; Orak, Tugba; Taşkın, Mesut; Adıgüzel, Ahmet; Özkan, Hakan

doi:10.1007/s12649-018-0468-6

Cited by 16 publications

(9 citation statements)

References 41 publications

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“…V B stands for the volume of NaOH used in the control cocktail (mL). The molarity of the NaOH solution employed in the titration (0.05 M) is N. The volume of the substrate cocktail solution (10 mL) is denoted by S. One unit (U) is the amount of lipase enzyme necessary to liberate 1 mol of fatty acids from triglycerides [5].…”

Section: Lipase Activity Calculationmentioning

confidence: 99%

“…Recently, environmental studies have investigated a new approach using lipase enzymes to clean septic tanks, grease traps, and other systems. Research had proven that lipase produced by some bacteria are capable of degrading FOG fat, oil, and grease) [5] Lipases are considered as one of the most important biocatalysts, whereby they can catalyze the reaction of ester hydrolysis, synthesis, esterification and transesterification. Recently, there has been a significant increase of interest in lipase production as it has the advantages of being active in the interfaces of organic compounds, produce high yield, while having low production cost, ease of genetic manipulation and has a broad substrate specificity.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, there has been a significant increase of interest in lipase production as it has the advantages of being active in the interfaces of organic compounds, produce high yield, while having low production cost, ease of genetic manipulation and has a broad substrate specificity. Microbial enzymes are also much more preferred than chemicals for hydrolytic reactions because they require less energy yet products are in higher quality [5,6] Lipases can be obtained from a variety of sources, including animal, vegetable, and microbial sources [1,5]. Lipases, also known as triacylglycerol acyl hydrolases (E.C.…”

Section: Introductionmentioning

confidence: 99%

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Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants

Mohaini

Farid

Muzammal

et al. 2022

Applied Microbiology

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Microbial lipase is one of the major sources of the enzyme that has been broadly exploited in the food, detergent, and pharmaceutical industries due to its high catalytic activity, high yield, and environmental friendliness and cost-effectiveness. Therefore, the aim of this study was to optimize the medium for the submerged fermentation for lipase production by a novel strain, Bacillus salmalaya strain 139SI. The media subjected to lipase production was Luria Bertani (LB) with different carbon sources and surfactants supplemented to determine which would give the highest lipase activity of Bacillus salmalaya. The Lipase activity of the supernatant containing lipase enzyme was ddetermined using the titrimetric method with hydrolysis reaction. Results showed that the olive oil that was used as a carbon source, induced the highest lipase activity (11.0 U/mL) compared to sunflower oil (9.6 U/mL) and cooking oil waste (7.8 U/mL). For surfactants, LB medium supplemented with tween 80 enhanced higher lipase activity (6.8 U/mL) compared to tween 20 (6.0 U/mL) and sodium dodecyl sulphate (SDS) (2.0 U/mL). Thus, it can be concluded that submerged fermentation allows optimization of the culture medium whereby, among carbon sources, olive oil induced the highest lipase production, whereas Tween 80 was the best lipase inducer compared to other surfactants.

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Section: Lipase Activity Calculationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants

Mohaini

Farid

Muzammal

et al. 2022

Applied Microbiology

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“…Bacillus licheniformis acts as a substitute for antibiotics and is among the most extensively used, direct‐fed growth promoters 23 . This study found that B. licheniformis improved the final body weight in CP ‐infected broilers after the stress of infection, which may be mainly attributed to the fact that B. licheniformis can generate several enzymes, such as amylase, protease, and lipase, and subsequently increase nutrient digestion and utilization in birds 24,25 . Furthermore, the alleviated effects of B. licheniformis on compromised body weight gain in CP ‐challenged broilers may contribute to the positive effects on immunity and intestinal barrier function.…”

Section: Discussionmentioning

confidence: 86%

“…23 This study found that B. licheniformis improved the final body weight in CP-infected broilers after the stress of infection, which may be mainly attributed to the fact that B. licheniformis can erate several enzymes, such as amylase, protease, and lipase, and subsequently increase nutrient digestion and utilization in birds. 24,25 Furthermore, the alleviated effects of B. licheniformis on compromised body weight gain in CP-challenged broilers may contribute to the positive effects on immunity and intestinal barrier function. The broiler immune system strongly protects against pathogenic organisms and resist the invasion of foreign substances in broilers.…”

Section: Discussionmentioning

confidence: 99%

The protective effects of Bacillus licheniformis against inflammatory responses and intestinal barrier damage in broilers with necrotic enteritis induced by Clostridium perfringens

Zhang

Qin²,

Yang

et al. 2023

J Sci Food Agric

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BackgroundBacillus licheniformis is a gram‐positive bacterium that has strong environmental adaptability and can improve the growth performance, immunity, and antioxidant function of broilers. The current study aimed to elucidate the protective capability of B. licheniformis against inflammatory responses and intestinal barrier damage in broilers with necrotic enteritis (NE) induced by Clostridium perfringens (CP).ResultsThe results showed that B. licheniformis enhanced the final body weight in broilers compared with that of broilers in the CP group after the stress of infection (P < 0.05). Bacillus licheniformis reversed the decreased levels of serum and jejunum mucosa immunoglobulins and anti‐inflammatory cytokines, reduced the values of villus height and the ratio of villus height to crypt depth, and mitigated the increased levels of serum d‐lactic acid and diamine oxidase in CP‐challenged broilers (P < 0.05). Moreover, B. licheniformis modulated the expression levels of genes involved in the TLR4/NF‐κB signalling pathway, the NLRP3 inflammasome activation pathway, and the sirt 1/Parkin signalling pathway in CP‐challenged broilers. Compared with the CP challenge group, the B. licheniformis‐treated group exhibited reduced abundance values of Shuttleworthia and Alistipes and enhanced abundance values of Parabacteroides in the caecal contents (P < 0.05).ConclusionBacillus licheniformis improved the final body weight and alleviated the inflammatory response and intestinal barrier function damage in birds with NE induced by CP by maintaining intestinal physiological function, enhancing immunity, regulating inflammatory cytokine secretion, modulating the mitophagy response, and increasing the abundance of beneficial intestinal flora. © 2023 Society of Chemical Industry.

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Raw starch degrading alkaline α‐amylase from Geobacillus kaustophilus TSCCA02: Production, characterization, and its potential for application as a detergent additive

Phonlamai,

Kingkaew,

Prajanket

et al. 2024

J Basic Microbiol

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Geobacillus kaustophilus TSCCA02, a newly isolated strain from cassava (Manihot esculenta L.) rhizosphere soil in Thailand, showed maximum raw starch degrading enzyme (RSDE) activity at 252.3 ± 9.32 U/mL with cassava starch and peptone at 5.0 and 3.0 g/L, respectively. 16 S ribosomal RNA (rRNA) sequencing and phylogenetic tree analyses indicated that the TSCCA02 strain was closely related to G. kaustophilus. The crude RSDE had optimal activity at 60°C and pH 9.0. This enzyme degraded various kinds of starch including potato starch, cassava starch, rice flour, corn starch, glutinous rice flour, and wheat flour to produce sugar syrup at 60°C, as confirmed by scanning electron microscopy (SEM), thin‐layer chromatography (TLC), and Fourier‐transform infrared spectroscopy (FTIR). The major end products of starch hydrolysis were maltose and maltotriose with a small amount of glucose, confirming this enzyme as an α‐amylase. The enzyme improved the washing efficiency of cotton fabric with commercial detergent. Results indicated the potential of alkaline α‐amylase produced from a new isolate of G. kaustophilus TSCCA02 for application as a detergent additive on an industrial scale.

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Enhancement of Amylase and Lipase Production from Bacillus licheniformis 016 Using Waste Chicken Feathers as Peptone Source

Cited by 16 publications

References 41 publications

Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants

Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants

The protective effects of Bacillus licheniformis against inflammatory responses and intestinal barrier damage in broilers with necrotic enteritis induced by Clostridium perfringens

Raw starch degrading alkaline α‐amylase from Geobacillus kaustophilus TSCCA02: Production, characterization, and its potential for application as a detergent additive

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