Aqueous Ethanol Extraction of Soybean Trypsin Inhibitors and Characterization of a Calcium-Sensitive Fraction

Liu, Keshun; Markakis, P.

doi:10.1111/j.1745-4514.1991.tb00152.x

Cited by 6 publications

(3 citation statements)

References 8 publications

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“…In grass peas, tempeh fermentation reduced the level of trypsin inhibitor by 99%, with the cooking step contributing to the greatest level of reduction (Stodolak & Starzynska‐Janiszewska, 2008). In soy, tempeh fermentation increased the antitryptic activity of the 85% ethanol extract, suggesting that tempeh fermentation released and increased the solubility of trypsin inhibitor compounds (Liu & Markakis, 1991).…”

Section: Resultsmentioning

confidence: 99%

Tempeh: A semicentennial review on its health benefits, fermentation, safety, processing, sustainability, and affordability

Ahnan-Winarno

Cordeiro

Winarno

et al. 2021

Comp Rev Food Sci Food Safe

131

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Tempeh is a fermented food made of mainly soybeans and is a nutritious, affordable, and sustainable functional source of protein. Globally, tempeh is a widely accepted fermented product. Although there is a growing body of literature on tempeh, most research has focused on unfermented soybeans, thus the impact of tempeh fermentation on biological properties of soybeans has been largely left scattered. The objective of this review is to summarize the literature of tempeh fermentation over the past 60 years. A search of articles on tempeh published from 1960 to 2020 was performed using the Cochrane Library, Web of Science, EBSCOhost FSTA database, and Google Scholar. References from identified articles were reviewed for additional sources. In total, 321 papers were selected for this review, of which 64 papers were related to the health benefits of tempeh. This review concluded that sufficient evidence exists in the literature supporting tempeh fermentation as a low‐cost, health‐promoting, and sustainable food processing technology to produce protein‐rich foods using various beans, legumes, and grains. This comprehensive review suggests further studies are needed on tempeh fermentation and its impact on human health; research and standardization of nonsoy tempeh; assessment of food safety‐improving modification in tempeh production system; and initiatives supporting the sourcing of local ingredients in tempeh production.

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Section: Resultsmentioning

confidence: 99%

Tempeh: A semicentennial review on its health benefits, fermentation, safety, processing, sustainability, and affordability

Ahnan-Winarno

Cordeiro

Winarno

et al. 2021

Comp Rev Food Sci Food Safe

131

View full text Add to dashboard Cite

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“…Second, the relative proportion of different inhibitors in a sample changed with species, varieties, processing method, and the degree of processing (Chen et al, 2014; DiPietro and Liener, 1981; Kumar et al, 2019). Third, a TIA assay method can also measure activity of non‐specific and non‐protein inhibitors (Liu and Markakis, 1991). Fourth, most trypsin inhibitors are proteins in nature.…”

Section: Resultsmentioning

confidence: 99%

Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

Liu

2021

J Americ Oil Chem Soc

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For expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement. With the proposed AOCS method Ba 12a-2020, four experiments were conducted, using four trypsin preparations having specific activity of 11,625, 12,602, 13,728, and 14,926 Nα-benzoyl-L-arginine ethyl ester (BAEE) units/mg protein, respectively. Experiment 1 determined the relationship between absorbance at 410 nm (A410) and trypsin concentration. Experiment 2 involved assaying raw and heated soybeans, expressing TIA as TUI/ mg sample and μg trypsin inhibited/mg sample, and determining conversion factors between the two units. Experiment 3 resembled Experiment 2 except for using purified soybean Kunitz inhibitor (KTI) and Bowman-Birk inhibitor (BBI). Conversion factors determined correlated highly with trypsin-specific activity (R 2 = 0.9789). After standardizing against a reference trypsin having 15,000 BAEE units/mg protein, a standardized conversion factor of 0.03 A410 (1.5 TUI) = 1 μg trypsin inhibited was determined. It remained consistent regardless of trypsin specific activity, with or without inhibitors, and type of inhibitor samples. By using purified inhibitors (Experiment 3), conversion values between TUI and μg trypsin inhibitor and between μg trypsin inhibited and μg trypsin inhibitor could also be calculated, enabling expression of TIA in amounts of pure KTI, BBI or their equivalents. Furthermore, when the AOCS method was modified with half substrate concentration, half trypsin concentration or half both (Experiment 4), TIA values in TUI could change with modifications but values in mg trypsin inhibited (standardized) or trypsin inhibitor remained consistent.

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“…Trypsin and chymotrypsin inhibitory proteins have been purified and characterized from a variety of legume seeds, e.g. pigeon pea (Godbole et al 1994), terary bean (Campos et al 1997), black gram (Padhye and Salunkhe 1980), red kidney bean (Wu and Whitaker 1990), soybean (Liu and Markakis 1991), Brazilian pink bean (Whitaker and Sgarbieri 1981), redgram (Mulimani and Paramjyothi 1992), seed of Clitoria ternatea (Macedo and Xavier-Filho 1992), Canavalia lineata (Terada et al 1994) and Phaseolus vulgaris L. (Carvalho and Sgarbieri 1997). Legume seeds normally contain trypsid chymotrypsin inhibitors of either the Bowman-Birk (10 kDa) or the Kunitz family (21 kDa) (Xavier-Filho and Campos 1989).…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Trypsin Inhibitors From Some Thai Legume Seeds

Benjakul

Visessanguan

Thummaratwasik

2000

J Food Biochemistry

103

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Trypsin inhibitors from cultivars of cowpea (Vigna unguiculata (L.) Wasp.), pigeon pea (Cajanus cajan (L.) Millsp.) and bambara groundnuts (Voandzeia subterranea (L.) Thou) grown in Thailand were isolated and characterized. Extraction of seeds with NaCl rendered a higher recovery of trypsin inhibitor than other solvents tested (P<0.05). The extraction time affected the inhibitor recovery (P<0.05). The extraction time of 3 h was optimum for the recovery of trypsin inhibitor from pigeon and bambara groundnuts, whereas 1 h was optimum for cowpea. Based cn inhibitor activity of zones separated by electrophoresis, the molecular mass of the inhibitor from bambara groundnuts was 13 kDa. Two inhibitory bands were observed for cowpea (10 and 18 kDa) and pigeon pea (15 and 25 kDa). Partial purification of inhibitors was achieved by heat‐treatment at 90C for 10 min, followed by ammonium sulfate precipitation with 30–65% saturation. The partially purified inhibitors from four seeds were heat stable up to 30 min at 90C at pH 7.0. The activities were also retained over a wide pH range at 25C but were lost when samples were treated with β‐mercaptoethanol prior to electrophoresis.

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Aqueous Ethanol Extraction of Soybean Trypsin Inhibitors and Characterization of a Calcium-Sensitive Fraction

Cited by 6 publications

References 8 publications

Tempeh: A semicentennial review on its health benefits, fermentation, safety, processing, sustainability, and affordability

Tempeh: A semicentennial review on its health benefits, fermentation, safety, processing, sustainability, and affordability

Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

Isolation and Characterization of Trypsin Inhibitors From Some Thai Legume Seeds

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