Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Zhang, Bin; Wang, Dongfeng; Wu, Hao; Zhang, Li; Ying, Xu

doi:10.1007/s13213-010-0056-x

Cited by 5 publications

(4 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Aflatoxin contamination to various agricultural crops, foods and feeds continues to be a serious quality and safety problem worldwide (20,21). Limiting the availability of simple sugars has been found to limit the ability of the fungus to produce aflatoxins (22). Hence, the alpha amylase inhibitors can be used to control the growth of A. flavus as well as the production of aflatoxins.…”

mentioning

confidence: 99%

An Isoquinoline Alkaloid, Berberine, Can Inhibit Fungal Alpha Amylase: Enzyme Kinetic and Molecular Modeling Studies

et al. 2012

View full text Add to dashboard Cite

Aspergillus flavus is a commonly found fungal pathogen, which produces aflatoxins, highly toxic and hepatocarcinogenic natural compounds. Inhibition of fungal alpha amylase activity has been found to limit the ability of the fungus to produce aflatoxins. Berberine, an isoquinoline alkaloid commonly found in many medicinal plants, was identified to inhibit the growth of A. flavus. The amount of berberine required to inhibit the fungal mycelial growth was determined. The compound was also found to inhibit the alpha amylase from the A. flavus. The binding affinity of the compound toward alpha amylase and the enzyme inhibitory activity have been determined by enzyme kinetic studies and Isothermal Titration Calorimetric analysis. Molecular modeling and docking studies were carried out to understand the enzyme–ligand interactions.

show abstract

mentioning

confidence: 99%

An Isoquinoline Alkaloid, Berberine, Can Inhibit Fungal Alpha Amylase: Enzyme Kinetic and Molecular Modeling Studies

et al. 2012

View full text Add to dashboard Cite

show abstract

“…The TI activity in CPCC fed in the current study was 22 TIU/mg, whereas the TI activity in cold-pressed soybean cake fed in the study by Woyengo et al (2016b) was 2.25 TIU/mg because it had been derived from heated soybean seeds. TIs can reduce the activities of proteases and carbohydrases (Zhang et al, 2010), leading to greater requirement of proteases and carbohydrases for nutrient digestion. Thus, the difference between the current study and that of Woyengo et al (2016b) with respect to the effect of multienzyme on nutrient digestibility could partly be due to differences in the TI activity in the evaluated feedstuffs, and hence optimal multienzyme dosage.…”

Section: Discussionmentioning

confidence: 99%

Nutritive value of multienzyme supplemented cold-pressed camelina cake for pigs

Woyengo

Patterson

Levesque

2018

Journal of Animal Science

View full text Add to dashboard Cite

Cold-pressed camelina cake (CPCC) is a fibrous co-product of camelina seed pressing and available for livestock feeding. However, information is lacking on the effect of supplementing fiber-degrading enzymes to CPCC-based diets on nutrient utilization by pigs. Experiment 1 determined the effect of multienzyme supplementation on standardized ileal digestibility (SID) of amino acid (AA) and net energy (NE) value of CPCC for pigs. Six ileal-cannulated barrows (average initial body weight [BW] = 36 kg) were fed five diets in 5 × 5 Latin square design with 1 added column to give six replicates per diet. The diets were a corn-soybean meal (SBM)-soybean oil-based diet and the basal diet with corn, SBM, and soybean oil replaced by 25% CPCC with or without multienzyme (600 U of xylanase, 75 U of glucanase, 250 U of cellulose, 30 U of mannanase, 350 U of invertase, 2,500 U of protease, and 6,000 U of amylase/kg of diet; Superzyme-CS, 0.5 g/kg) in a 2 × 2 factorial arrangement. The fifth diet was a low-casein cornstarch-based diet. The ratio of corn to SBM and soybean oil in the basal diet was identical to the CCPC-containing diets to allow calculation of nutrient digestibility of CPCC by the difference method. On a dry matter (DM) basis, CPCC contained 42% crude protein, 10.5% ether extract, 25.4% neutral detergent fiber (NDF), 2.07% Lys, 0.73% Met, 1.64% Thr, 0.51% Trp, and 22.1 trypsin inhibitor units per milligram, respectively. The SID of Lys, Met, Thr, and Trp for CPCC were 43.5%, 70.7%, 44.8%, and 55.3%, respectively. The digestible energy (DE) and NE values for CPCC were 3,663 and 2,209 kcal/kg of DM, respectively. Multienzyme supplementation did not affect the SID of AA, and DE and NE values for the corn-SBM-CPCC-based diet, and for the CPCC. In experiment 2, the effects of multienzyme dosage (0.5 or 50 g/kg of treated feedstuff) on porcine in vitro digestibility of DM (IVDDM) of CPCC was determined. The IVDDM of CPCC was increased (P < 0.001) with an increase in multienzyme dosage. Multienzyme at 0.5 g/kg did not affect IVDDM of CPCC. However, multienzyme at 50 g/kg increased (P < 0.01) IVDDM for CPCC by at least 16%. In conclusion, multienzyme at 0.5 g/kg did not affect SID of AA and NE values, and IVDDM for CPCC. However, multienzyme at 50 g/kg improved IVDDM of CPCC, implying that the efficacy of the multienzyme with regard to improving nutrient digestibility of CPCC in pigs is dosage dependent.

show abstract

“…flavus-resistant plants. 64 A proteinase inhibitor was characterised as a Bowman-Birk type inhibitor from seeds of Vigna mungo. 65 In barley, Barley trypsin inhibitors-Chloroform/Methanol type TI and 13 cystatins (HvCPI-1 to 13) have been reported to inhibit the digestive proteases of pests as well as in vitro fungal growth.…”

Section: Endogenous Ppismentioning

confidence: 99%

“…Lethal concentrations of SBTI/WBTI limit the hydrolysing activity of α‐amylase and further accumulation of aflatoxin B1. Furthermore, TI genes from soybean (domesticated and wild‐type) could be used to develop anti‐ A. flavus‐ resistant plants 64 . A proteinase inhibitor was characterised as a Bowman‐Birk type inhibitor from seeds of Vigna mungo 65 …”

Section: Endogenous Ppismentioning

confidence: 99%

Evaluating the pesticidal impact of plant protease inhibitors: lethal weaponry in the co‐evolutionary battle

Pandey

Yadav

Sanyal

2021

Pest Management Science

View full text Add to dashboard Cite

In the arsenal of plant defense, protease inhibitors (PIs) are well-designed defensive products to counter field pests. PIs are produced in plant tissues by means of 'stable defense metabolite' and triggered on demand as the perception of the signal and well established as a part of plant active defense. PIs have been utilized for approximately four decades, initially as a gene-alone approach that was later replaced by multiple gene pyramiding/gene stacking due to insect adaptability towards the PI alone. By considering the adaptive responses of the pest to the single insecticidal gene, the concept of gene pyramiding gained continuous appreciation for the development of transgenic crops to deal with co-evolving pests. Gene pyramiding approaches are executed to bypass the insectʼs adaptive responses against PIs. Stacking PIs with additional insecticidal proteins, plastid engineering, recombinant proteinase inhibitors, RNAi-based methods and CRISPR/Cas9-mediated genome editing are the advanced tools and methods for next-generation pest management. Undoubtedly, the domain associated with the mechanism of PIs in the course of plant-pest interactions will occupy a central role for the advancement of more efficient and sustainable pest control strategies.

show abstract

Inhibition of endogenous α-amylase and protease of Aspergillus flavus by trypsin inhibitor from cultivated and wild-type soybean

Cited by 5 publications

References 35 publications

An Isoquinoline Alkaloid, Berberine, Can Inhibit Fungal Alpha Amylase: Enzyme Kinetic and Molecular Modeling Studies

An Isoquinoline Alkaloid, Berberine, Can Inhibit Fungal Alpha Amylase: Enzyme Kinetic and Molecular Modeling Studies

Nutritive value of multienzyme supplemented cold-pressed camelina cake for pigs

Evaluating the pesticidal impact of plant protease inhibitors: lethal weaponry in the co‐evolutionary battle

Contact Info

Product

Resources

About