The origin of honey amylase

Rinaudo, M.; Ponzetto, Carola; Vidano, C.; Marletto, Franco

doi:10.1016/0305-0491(73)90315-5

Cited by 9 publications

(7 citation statements)

References 1 publication

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“…Their determination was based on observation of color change qualitatively, which could have compromised the sensitivity of their assessment. Rinaudo and others (1973) reported a temperature optimum of 46 °C and a wide range of 45 to 60 °C for the honey amylase and bee amylase, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…The origin of amylase in honey has been attributed to the salivary secretions of bees. This conclusion was based on the presence of amylase in honey produced by sugar‐fed bees (Stadelmeier and Bergner 1986) and on similarities between honey amylase and bee amylase (Rinaudo and others 1973). These similarities included the need for chloride ions for catalytic activity, inhibition by acetylating agents, and similar sensitivity to pH by bee and honey amylases when compared to nectar and pollen amylases (Rinaudo and others 1973).…”

Section: Introductionmentioning

confidence: 99%

“…This conclusion was based on the presence of amylase in honey produced by sugar‐fed bees (Stadelmeier and Bergner 1986) and on similarities between honey amylase and bee amylase (Rinaudo and others 1973). These similarities included the need for chloride ions for catalytic activity, inhibition by acetylating agents, and similar sensitivity to pH by bee and honey amylases when compared to nectar and pollen amylases (Rinaudo and others 1973). We have previously purified the major amylase from honey utilizing gel filtration followed by ion exchange chromatography (Babacan and Rand 2005).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Honey Amylase

Babacan

Rand

2007

Journal of Food Science

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The major alpha-amylase in honey was characterized. The optimum pH range and temperature were determined for the enzyme as 4.6 to 5.3 and 55 degrees C, respectively. The enzyme was stable at pH values from 7 to 8. The half-lives of the purified enzyme at different temperatures were determined. The activation energy for heat inactivation of honey amylase was 114.6 kJ/mol. The enzyme exhibited Michaelis-Menten kinetics with soluble starch and gave KM and Vmax values of 0.72 mg/mL and 0.018 units/mL, respectively. The enzyme was inhibited by CuCl (34.3%), MgCl2 (22.4%), and HgCl2 (13.4%), while CaCl2, MnCl2, and ZnSO4 did not have any effect. Starch had a protective effect on thermal stability of honey amylase. Therefore, it might be critical to process or control the amylase in honey before incorporation into starch-containing foods to aid in the preservation of starch functionality. One step could involve heat treating honey with other ingredients, especially those that dilute and acidify the honey environment.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization of Honey Amylase

Babacan

Rand

2007

Journal of Food Science

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“…Today, the most widely accepted theory attributes the origin of diastase in honey to salivary secretions of bees. This conclusion is based on the presence of diastase in honey produced by sugar-fed bees, and on the similarity between honey diastase and bee diastase (Ammon, 1949;Rinaudo et al, 1973;Stadelmeier and Bergner, 1986). However, this does not explain why honeys of diverse botanical origin show a different diastatic activity, a fact which has been known for many years (Lothrop and Paine, 1931 (Sipos, 1964), or seasonal activity of the pharyngeal glands (Halberstadt, 1980;Fluri et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Diastatic activity in some unifloral honeys

Oddo

Baldi²,

Accorti

1990

Apidologie

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Summary — Determinations of diastatic activity in 12 groups of unifloral honey were made to study variability according to the botanical origin of the honey. Robinia, Citrus, Erica, Taraxacum and Arbutus honeys were found to have a very low enzyme content. On the contrary Hedysarum, Castanea, Honeydew, Eucalyptus and Thymus honeys showed high diastase activity. The relationship between the absorbance at 5 min and the diastatic index was quantified.

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“…Amylase helps to digest carbohydrates, while protease and lipase digest bee bread into amino acids and lipids, which bees can absorb (Howell, 1985). Rinaudo et al (1973) compared the properties and characteristics of honey bee food glands, including nectar and honey amylase. Their results indicate that honey amylase is secreted by honey bee food glands, rather than obtained from pollen and nectar.…”

Section: Introductionmentioning

confidence: 99%

Bacillus in the guts of honey bees (Apis mellifera; Hymenoptera: Apidae) mediate changes in amylase values

Wang¹,

Zhao²,

Xu³

et al. 2015

Eur. J. Entomol.

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Abstract. Amylase is one of three main enzymes involved in the breakdown and utilization of macromolecules. In honey bees (Apis mellifera), amylase was traditionally believed to originate only as secretion of the bee. However, other sources of amylase production, such as microbes in the guts of bees remained to be studied. In our research, we compared the differences in the amylase values in rape flower nectar and honey in the stomachs of bees. Then, culture-dependent and culture-independent (16sDNA) methods were used to isolate and identify bacteria in rape flower nectar and bee stomach honey. The dominant bacteria were added to nectar, and the amylase values of nectar with added gut microbes and nectar without added microbes were compared. Our findings indicate that the amylase value was significantly increased, which correlates with the increase in number of bacteria that occurred from nectar to honey in the stomachs of bees. The dominant bacteria in honey bee stomachs were mainly Bacillus during the flowering season of rape. Experiments confirmed that the amylase levels in nectar increased significantly when bacteria were added. These results indicate that bacteria in the foregut of bees help in the processing floral nectar into honey.

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The origin of honey amylase

Cited by 9 publications

References 1 publication

Characterization of Honey Amylase

Characterization of Honey Amylase

Diastatic activity in some unifloral honeys

Bacillus in the guts of honey bees (Apis mellifera; Hymenoptera: Apidae) mediate changes in amylase values

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